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Database: UniProt
Entry: A0A198GBN6_9GAMM
LinkDB: A0A198GBN6_9GAMM
Original site: A0A198GBN6_9GAMM 
ID   A0A198GBN6_9GAMM        Unreviewed;       397 AA.
AC   A0A198GBN6;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Probable peptidoglycan glycosyltransferase FtsW {ECO:0000256|HAMAP-Rule:MF_00913};
DE            Short=PGT {ECO:0000256|HAMAP-Rule:MF_00913};
DE            EC=2.4.1.129 {ECO:0000256|HAMAP-Rule:MF_00913};
DE   AltName: Full=Cell division protein FtsW {ECO:0000256|HAMAP-Rule:MF_00913};
DE   AltName: Full=Cell wall polymerase {ECO:0000256|HAMAP-Rule:MF_00913};
DE   AltName: Full=Peptidoglycan polymerase {ECO:0000256|HAMAP-Rule:MF_00913};
DE            Short=PG polymerase {ECO:0000256|HAMAP-Rule:MF_00913};
GN   Name=ftsW {ECO:0000256|HAMAP-Rule:MF_00913};
GN   ORFNames=M983_0913 {ECO:0000313|EMBL:OAT34842.1};
OS   Proteus myxofaciens ATCC 19692.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=1354337 {ECO:0000313|EMBL:OAT34842.1, ECO:0000313|Proteomes:UP000094023};
RN   [1] {ECO:0000313|EMBL:OAT34842.1, ECO:0000313|Proteomes:UP000094023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19692 {ECO:0000313|EMBL:OAT34842.1,
RC   ECO:0000313|Proteomes:UP000094023};
RA   Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT   "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT   the evolutionary history of the Enterobacteriaceae.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Peptidoglycan polymerase that is essential for cell division.
CC       {ECO:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00023988, ECO:0000256|HAMAP-
CC         Rule:MF_00913};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00913}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00913}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00913}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}. Note=Localizes to the
CC       division septum. {ECO:0000256|HAMAP-Rule:MF_00913}.
CC   -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily.
CC       {ECO:0000256|ARBA:ARBA00038053, ECO:0000256|HAMAP-Rule:MF_00913}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00913}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAT34842.1}.
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DR   EMBL; LXEN01000039; OAT34842.1; -; Genomic_DNA.
DR   RefSeq; WP_066747719.1; NZ_LXEN01000039.1.
DR   AlphaFoldDB; A0A198GBN6; -.
DR   STRING; 1354337.M983_0913; -.
DR   PATRIC; fig|1354337.4.peg.931; -.
DR   OrthoDB; 9768187at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000094023; Unassembled WGS sequence.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IPR018365; Cell_cycle_FtsW-rel_CS.
DR   InterPro; IPR013437; FtsW.
DR   InterPro; IPR001182; FtsW/RodA.
DR   NCBIfam; TIGR02614; ftsW; 1.
DR   PANTHER; PTHR30474; CELL CYCLE PROTEIN; 1.
DR   PANTHER; PTHR30474:SF2; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE FTSW-RELATED; 1.
DR   Pfam; PF01098; FTSW_RODA_SPOVE; 1.
DR   PROSITE; PS00428; FTSW_RODA_SPOVE; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00913}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00913};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00913};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00913};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00913}; Reference proteome {ECO:0000313|Proteomes:UP000094023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00913};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00913}.
FT   TRANSMEM        31..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        96..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        205..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        281..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        326..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT   TRANSMEM        359..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
SQ   SEQUENCE   397 AA;  43933 MW;  A6F6717EBBE5E43A CRC64;
     MSLSVMRRLK QWLVGSYQTE NTAFVPYDRT LLWFTFGLAV VGFVMVTSAS MPVGQRLAED
     PFFFAKRDGI YIIVALCIAL VTMRIPMAVW QRYSSLMLFG SILLLLVVLA VGSSVNGASR
     WIALGPLRVQ PAELSKLALF CYLSSYLVRK VEEVRNNFWG FCKPMGVMLI LAVLLLLQPD
     LGTVVVLFVT TLALLFLAGA KIWQFLAIIG SGIAAVVMLI IVEPYRVRRI TSFLEPWDDP
     FGSGYQLTQS LMAFGRGDLL GQGLGNSVQK LEYLPEAHTD FIFAILAEEL GYIGVVLVLL
     MVFFIAFRAM QIGRRALILE QRFSGFLACS IGIWFTFQTL VNVGAAAGML PTKGLTLPLI
     SYGGSSLIIM STAIVMLLRI DYETRLAQAQ AFVRSPK
//
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