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FTSW_METMM
ID   FTSW_METMM              Reviewed;         388 AA.
AC   F9ZZQ0;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Probable peptidoglycan glycosyltransferase FtsW {ECO:0000255|HAMAP-Rule:MF_00913};
DE            Short=PGT {ECO:0000255|HAMAP-Rule:MF_00913};
DE            EC=2.4.1.129 {ECO:0000255|HAMAP-Rule:MF_00913};
DE   AltName: Full=Cell division protein FtsW {ECO:0000255|HAMAP-Rule:MF_00913};
DE   AltName: Full=Cell wall polymerase {ECO:0000255|HAMAP-Rule:MF_00913};
DE   AltName: Full=Peptidoglycan polymerase {ECO:0000255|HAMAP-Rule:MF_00913};
DE            Short=PG polymerase {ECO:0000255|HAMAP-Rule:MF_00913};
GN   Name=ftsW {ECO:0000255|HAMAP-Rule:MF_00913}; OrderedLocusNames=Metme_0260;
OS   Methylomonas methanica (strain MC09).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomonas.
OX   NCBI_TaxID=857087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC09;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Stein L., Woyke T.;
RT   "Complete sequence of Methylomonas methanica MC09.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Peptidoglycan polymerase that is essential for cell division.
CC       {ECO:0000255|HAMAP-Rule:MF_00913}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00913};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00913}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00913}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00913}. Note=Localizes to the division septum.
CC       {ECO:0000255|HAMAP-Rule:MF_00913}.
CC   -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00913}.
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DR   EMBL; CP002738; AEF98709.1; -; Genomic_DNA.
DR   RefSeq; WP_013816982.1; NC_015572.1.
DR   AlphaFoldDB; F9ZZQ0; -.
DR   SMR; F9ZZQ0; -.
DR   STRING; 857087.Metme_0260; -.
DR   EnsemblBacteria; AEF98709; AEF98709; Metme_0260.
DR   KEGG; mmt:Metme_0260; -.
DR   eggNOG; COG0772; Bacteria.
DR   HOGENOM; CLU_029243_1_1_6; -.
DR   OMA; KLWWSNL; -.
DR   OrthoDB; 1133883at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008888; Chromosome.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_00913; PGT_FtsW_proteobact; 1.
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.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW   Peptidoglycan synthesis; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..388
FT                   /note="Probable peptidoglycan glycosyltransferase FtsW"
FT                   /id="PRO_0000415198"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        41..57
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        79..85
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        107..117
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        138..147
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        169..170
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        214..271
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        293..315
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        337..348
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT   TOPO_DOM        370..388
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   388 AA;  41979 MW;  954224F9E36F2FA9 CRC64;
     MSAAAPKPRP AHRFHIDQTL LSVCLCLLGI GFVMVASSSM HLGVKMADDV SYYPFKQLVH
     IILGLMFAAA ILAIPMKYWQ KIGQPLFIVG LVLLLVVLIP GVGVKVNGST RWLSLLGLRI
     QVSEVMKFIS VVYMAGYITR HSDHVRHSIF GLLRPLMLLS VASILLLLEP DFGSAVVILI
     IAMGMMFLGG ARLSPFVALV ALISSAGAIL ASSADYRVKR MTSFLNPWEH ARDSGYQLTQ
     ALISFGRGEV SGVGLGNGLQ KLFYLPEAHT DFLFSVLGEE LGLVGVTLVI ALFTTLVVRG
     FSIGEQAEAA GERFSALVAY GLVIWFGFQA FVNMGVNMGI LPTKGLTLPL MSYGGGSMIV
     MCGAMAVLFR IHYEVTELHK SNIKGKSR
 
 
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