ID I1DUI8_9GAMM Unreviewed; 403 AA.
AC I1DUI8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
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 ECO:0000313|EMBL:GAB57716.1};
GN ORFNames=RNAN_0685 {ECO:0000313|EMBL:GAB57716.1};
OS Rheinheimera nanhaiensis E407-8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=562729 {ECO:0000313|EMBL:GAB57716.1, ECO:0000313|Proteomes:UP000004374};
RN [1] {ECO:0000313|EMBL:GAB57716.1, ECO:0000313|Proteomes:UP000004374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E407-8 {ECO:0000313|EMBL:GAB57716.1,
RC ECO:0000313|Proteomes:UP000004374};
RX PubMed=23209246; DOI=10.1128/JB.01922-12;
RA Zhang X.-Y., Zhang Y.-J., Qin Q.-L., Xie B.-B., Chen X.-L., Zhou B.-C.,
RA Zhang Y.-Z.;
RT "Genome Sequence of the Protease-Producing Bacterium Rheinheimera
RT nanhaiensis E407-8T, Isolated from Deep-Sea Sediment of the South China
RT Sea.";
RL J. Bacteriol. 194:7001-7002(2012).
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: 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:GAB57716.1}.
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DR EMBL; BAFK01000003; GAB57716.1; -; Genomic_DNA.
DR RefSeq; WP_008218736.1; NZ_BAFK01000003.1.
DR AlphaFoldDB; I1DUI8; -.
DR STRING; 562729.RNAN_0685; -.
DR OrthoDB; 9768187at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000004374; 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; 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.
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};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW 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|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:UP000004374};
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 35..54
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 74..92
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 99..117
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 129..153
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 165..182
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 188..205
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 210..228
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 286..311
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 331..355
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 361..383
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
SQ SEQUENCE 403 AA; 44406 MW; 433666E53A3B8DE1 CRC64;
MKQLALSMFK QPWANPLQAL SQWWRAEDGA AYDKLFLTLL LLILAIGVVM VTSASVPVAS
RLYDNELHFT IRHLVYLALG CTAALIILNI PVQWWHNSNM ALLFAALALL VAVLLFGRNV
NGSTRWLSLG FFGLQAAEPA KLFFFVYLAS YLVRRHEEVR ENLKGFLKPL FVLFAFAVLL
LMQPDLGTVI VMFATAVALL FLAGAKLWQF FCLIFTGIAA IGVLIVYSEY RWKRVTAFLD
PWADPFGSGY QLTQSLMAFG RGGWFGQGLG NSIQKLEYLP EAHTDFILAV IAEETGFIGV
AVLVLLLFLL VYRALWIGQR ALAKNLSFHG FLAYALAIWI GFQSAVNIGV ATGALPTKGL
TLPYVSSGGS SLIIMLAAAA LLLRIDFEVR LKGKHAISGG KHD
//
