ID U3U7P8_9GAMM Unreviewed; 404 AA.
AC U3U7P8;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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:BAO00447.1};
GN ORFNames=HHS_04770 {ECO:0000313|EMBL:BAO00447.1};
OS Candidatus Pantoea carbekii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=1235990 {ECO:0000313|EMBL:BAO00447.1, ECO:0000313|Proteomes:UP000016900};
RN [1] {ECO:0000313|EMBL:BAO00447.1, ECO:0000313|Proteomes:UP000016900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kobayashi H., Fujii-Muramatsu R., Takeishi K., Noda H.;
RT "Genome sequence of the symbiont of the pentatomidae stink bug Halyomorpha
RT halys.";
RL Submitted (OCT-2012) 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}.
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DR EMBL; AP012554; BAO00447.1; -; Genomic_DNA.
DR AlphaFoldDB; U3U7P8; -.
DR STRING; 1235990.BMSBPS_0102; -.
DR KEGG; hhs:HHS_04770; -.
DR PATRIC; fig|1235990.3.peg.473; -.
DR eggNOG; COG0772; Bacteria.
DR OrthoDB; 9768187at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000016900; Chromosome.
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|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:UP000016900};
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 38..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 76..97
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 103..125
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 212..232
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 297..318
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 362..385
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
SQ SEQUENCE 404 AA; 45832 MW; BBD05A09AC12799D CRC64;
MRISKIHIAH LLPLCFKHWI KNVYKHNNVS VVLYDRTLLL LTFGLTIIGL IMITSASMPT
SEHLNEDPFY FTKRHILYIA IAFSIVIITL RLPMHFWQRY SNIMLILSVF MLIFVLIIGI
AVNGASRWIP LGPFRIQPGE LSKFSLCCYL ASYFVRKVDE VRNNFWGFCK PITIMILLSL
LLLAEPDFGT AIVLFVTTLV MLFLVGAKVW QYIIIIMSSI LIVMPLIIAK PYRLHRIISF
WNPWHDPFGS GYQLTQSLMA FGRGQLWGQG LGNSVQKLEY LPESYTDFIF SILGEELGYV
GVVLVLLMIC FVALRALSIG RRALEMNQNF SGFLACSIGI WFSLQVLVNI GSASGMLPTK
GLTLPLISYG GSSFIIIATA IVCLLRTDYE TRLAKMHLCN RITR
//
