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FTSW_BACSU
ID   FTSW_BACSU              Reviewed;         403 AA.
AC   O07639;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 123.
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:0000305};
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; Synonyms=ylaO; OrderedLocusNames=BSU14850;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Purnelle B., Presecan E., Glaser P., Richou A., Danchin A., Goffeau A.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION IN CELL DIVISION, AND INDUCTION.
RC   STRAIN=168;
RX   PubMed=17526699; DOI=10.1128/jb.00467-07;
RA   Lu Z., Takeuchi M., Sato T.;
RT   "The LysR-type transcriptional regulator YofA controls cell division
RT   through the regulation of expression of ftsW in Bacillus subtilis.";
RL   J. Bacteriol. 189:5642-5651(2007).
CC   -!- FUNCTION: Peptidoglycan polymerase that is essential for cell division.
CC       {ECO:0000250|UniProtKB:P39604, ECO:0000305|PubMed:17526699}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC         Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC         (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC         cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC         D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC         diphosphate + 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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P39604};
CC       Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the
CC       division septum.
CC   -!- INDUCTION: Expression is regulated by YofA.
CC       {ECO:0000269|PubMed:17526699}.
CC   -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily. {ECO:0000305}.
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DR   EMBL; Z97025; CAB09720.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13358.1; -; Genomic_DNA.
DR   PIR; E69873; E69873.
DR   RefSeq; NP_389368.1; NC_000964.3.
DR   RefSeq; WP_009967159.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O07639; -.
DR   SMR; O07639; -.
DR   IntAct; O07639; 9.
DR   STRING; 224308.BSU14850; -.
DR   PaxDb; O07639; -.
DR   EnsemblBacteria; CAB13358; CAB13358; BSU_14850.
DR   GeneID; 935918; -.
DR   KEGG; bsu:BSU14850; -.
DR   PATRIC; fig|224308.179.peg.1619; -.
DR   eggNOG; COG0772; Bacteria.
DR   InParanoid; O07639; -.
DR   OMA; KLWWSNL; -.
DR   PhylomeDB; O07639; -.
DR   BioCyc; BSUB:BSU14850-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001570; 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; IPR001182; FtsW/RodA.
DR   PANTHER; PTHR30474; PTHR30474; 1.
DR   Pfam; PF01098; FTSW_RODA_SPOVE; 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..403
FT                   /note="Probable peptidoglycan glycosyltransferase FtsW"
FT                   /id="PRO_0000062723"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..51
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..80
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..108
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..141
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..165
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..189
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        211..285
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        307..309
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        352..354
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        376..403
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   403 AA;  43732 MW;  AA851E1CBD8DE9A8 CRC64;
     MLKKMLKSYD YSLIFAIVLL CGFGLVMVYS SSMITAVSRY GVSSNFFFMR QLFALIAGGA
     LFILMALFPY KALAHQKFQK GILLVSVLAL ISLFVFGHVA GNAQSWFKIG GMSIQPGEFV
     KLVVILYLAA VYAKKQSYID HLLTGVAPPV VMTLIICGLI AMQPDFGTAM IIGLIATCMI
     LCSGFSGKTL VRLVILGGIV FILVSPIIYL NQDKILTEGR LARFESLEDP FKYANSSGLQ
     VINSYYAISS GGIFGLGLGE SIQKYGYLPE SHTDFIMAVI AEELGIFGVL FVIFLLGFVV
     IKGFYIARKC EDPFGSLLAI GISSMIAIQS FINLGGVSGL IPITGVTLPF ISYGGSSLVL
     LLGSMGILAN ISMFVKYSEN KKKKEPLAPK GMKKKQLKKT VYL
 
 
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