ID   FTSW_MYCTU              Reviewed;         524 AA.
AC   P9WN97; L0T901; O06223; P63762;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   11-DEC-2019, entry version 30.
DE   RecName: Full=Probable peptidoglycan glycosyltransferase FtsW {ECO:0000250|UniProtKB:P39604};
DE            Short=PGT {ECO:0000250|UniProtKB:P39604};
DE            EC=2.4.1.129 {ECO:0000250|UniProtKB:P39604};
DE   AltName: Full=Cell division protein FtsW {ECO:0000250|UniProtKB:O07639};
DE   AltName: Full=Cell wall polymerase {ECO:0000250|UniProtKB:P39604};
DE   AltName: Full=Peptidoglycan polymerase {ECO:0000250|UniProtKB:P39604};
DE            Short=PG polymerase {ECO:0000250|UniProtKB:P39604};
GN   Name=ftsW; OrderedLocusNames=Rv2154c; ORFNames=MTCY270.14;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   INTERACTION WITH FTSZ, AND DOMAIN.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=12101218; DOI=10.1074/jbc.m203847200;
RA   Datta P., Dasgupta A., Bhakta S., Basu J.;
RT   "Interaction between FtsZ and FtsW of Mycobacterium tuberculosis.";
RL   J. Biol. Chem. 277:24983-24987(2002).
RN   [3]
RP   SUBUNIT, INTERACTION WITH PBPB, SUBCELLULAR LOCATION, TOPOLOGY, AND DOMAIN.
RX   PubMed=17427288; DOI=10.1111/j.1365-2958.2006.05491.x;
RA   Datta P., Dasgupta A., Singh A.K., Mukherjee P., Kundu M., Basu J.;
RT   "Interaction between FtsW and penicillin-binding protein 3 (PBP3) directs
RT   PBP3 to mid-cell, controls cell septation and mediates the formation of a
RT   trimeric complex involving FtsZ, FtsW and PBP3 in mycobacteria.";
RL   Mol. Microbiol. 62:1655-1673(2006).
CC   -!- FUNCTION: Peptidoglycan polymerase that is essential for cell division.
CC       {ECO:0000250|UniProtKB:P39604}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC         Ala)](n)-diphospho-di-trans,octa-cis-undecaprenol + beta-D-GlcNAc-
CC         (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-
CC         trans,octa-cis-undecaprenol = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC         D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-diphospho-di-trans-octa-cis-
CC         undecaprenol + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC         Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC         ChEBI:CHEBI:78435; EC=2.4.1.129;
CC         Evidence={ECO:0000250|UniProtKB:P39604};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000250|UniProtKB:P39604}.
CC   -!- SUBUNIT: Forms a complex with FtsZ and PbpB (PBP3, FtsI).
CC       {ECO:0000269|PubMed:17427288}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17427288};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:17427288}.
CC       Note=Localizes to the division septum. {ECO:0000250}.
CC   -!- DOMAIN: Interacts with FtsZ via its C-terminal region, and with PbpB
CC       via two extracytoplasmic loops. {ECO:0000269|PubMed:12101218,
CC       ECO:0000269|PubMed:17427288}.
CC   -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily. {ECO:0000305}.
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DR   EMBL; AL123456; CCP44930.1; -; Genomic_DNA.
DR   PIR; F70579; F70579.
DR   RefSeq; NP_216670.1; NC_000962.3.
DR   RefSeq; WP_003411165.1; NZ_NVQJ01000044.1.
DR   STRING; 83332.Rv2154c; -.
DR   PaxDb; P9WN97; -.
DR   EnsemblBacteria; CCP44930; CCP44930; Rv2154c.
DR   GeneID; 887916; -.
DR   KEGG; mtu:Rv2154c; -.
DR   KEGG; mtv:RVBD_2154c; -.
DR   TubercuList; Rv2154c; -.
DR   eggNOG; ENOG4105CNI; Bacteria.
DR   eggNOG; COG0772; LUCA.
DR   KO; K03588; -.
DR   OMA; KLWWSNL; -.
DR   PhylomeDB; P9WN97; -.
DR   BioCyc; MTBH37RV:G185E-6362-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IBA:GO_Central.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR   InterPro; IPR018365; Cell_cycle_FtsW-rel_CS.
DR   InterPro; IPR013437; FtsW.
DR   InterPro; IPR001182; FtsW/RodA.
DR   PANTHER; PTHR30474; PTHR30474; 1.
DR   Pfam; PF01098; FTSW_RODA_SPOVE; 1.
DR   TIGRFAMs; TIGR02614; ftsW; 1.
DR   PROSITE; PS00428; FTSW_RODA_SPOVE; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW   Peptidoglycan synthesis; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..524
FT                   /note="Probable peptidoglycan glycosyltransferase FtsW"
FT                   /id="PRO_0000062725"
FT   TOPO_DOM        1..55
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..89
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..121
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        143..151
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        173..191
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        234
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        256..311
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..350
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        351..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        374..388
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        389..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        410..524
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   524 AA;  56337 MW;  C98052A346739C7C CRC64;
     MLTRLLRRGT SDTDGSQTRG AEPVEGQRTG PEEASNPGSA RPRTRFGAWL GRPMTSFHLI
     IAVAALLTTL GLIMVLSASA VRSYDDDGSA WVIFGKQVLW TLVGLIGGYV CLRMSVRFMR
     RIAFSGFAIT IVMLVLVLVP GIGKEANGSR GWFVVAGFSM QPSELAKMAF AIWGAHLLAA
     RRMERASLRE MLIPLVPAAV VALALIVAQP DLGQTVSMGI ILLGLLWYAG LPLRVFLSSL
     AAVVVSAAIL AVSAGYRSDR VRSWLNPEND PQDSGYQARQ AKFALAQGGI FGDGLGQGVA
     KWNYLPNAHN DFIFAIIGEE LGLVGALGLL GLFGLFAYTG MRIASRSADP FLRLLTATTT
     LWVLGQAFIN IGYVIGLLPV TGLQLPLISA GGTSTAATLS LIGIIANAAR HEPEAVAALR
     AGRDDKVNRL LRLPLPEPYL PPRLEAFRDR KRANPQPAQT QPARKTPRTA PGQPARQMGL
     PPRPGSPRTA DPPVRRSVHH GAGQRYAGQR RTRRVRALEG QRYG
//