ID A4G8T9_HERAR Unreviewed; 402 AA.
AC A4G8T9;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 2.
DT 24-JAN-2024, entry version 87.
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:CAL62926.2};
GN OrderedLocusNames=HEAR2812 {ECO:0000313|EMBL:CAL62926.2};
OS Herminiimonas arsenicoxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL62926.2, ECO:0000313|Proteomes:UP000006697};
RN [1] {ECO:0000313|EMBL:CAL62926.2, ECO:0000313|Proteomes:UP000006697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(2007).
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; CU207211; CAL62926.2; -; Genomic_DNA.
DR AlphaFoldDB; A4G8T9; -.
DR STRING; 204773.HEAR2812; -.
DR KEGG; har:HEAR2812; -.
DR eggNOG; COG0772; Bacteria.
DR HOGENOM; CLU_029243_1_1_4; -.
DR OrthoDB; 9768187at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006697; 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; 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}; 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:UP000006697};
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 33..55
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 67..88
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 100..119
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 139..155
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 167..184
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 190..207
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 214..232
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 290..314
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 326..350
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 370..389
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
SQ SEQUENCE 402 AA; 44222 MW; 2F8C72E6C4726094 CRC64;
MKFAFPSFSS AAAQKAVTSL DQRSKMMAYD QPLVWVVVLL MLFGMVMVYS ASISLPDSPK
YARYDNAHFV TRQAMFISVS LIAGLLAFRV RMETWQKLAP YLFVATLILL VLVLVPGVGK
GVNGARRWLS FKVFNLQPSE LMKLFVVLYA ADYTVRKQQV MHKLTKGFMP MTLAIGFVGL
LLLLEPDLGA FGVIVCIAMG ILFLGGINGI WFGGIGATLV GIFSMVILLS PWRRERIFAY
LNPWEEENAL GKAYQLSHSL IAFGRGELFG VGLGGSVEKL HYLPEAHTDF LLAVIGEELG
FVGVFVVIAL FYWIIKRSFE IGRQAIAMDL TFAGLVAKGI GIWIGVQAFI NMGVNLGLLP
TKGLTLPLMS YGGSGVLINC IGLAILLRID YENRVLMRGG RI
//
