ID A0A4R6Y679_9BURK Unreviewed; 403 AA.
AC A0A4R6Y679;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=DFR44_11634 {ECO:0000313|EMBL:TDR30836.1};
OS Hydromonas duriensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Hydromonas.
OX NCBI_TaxID=1527608 {ECO:0000313|EMBL:TDR30836.1, ECO:0000313|Proteomes:UP000294480};
RN [1] {ECO:0000313|EMBL:TDR30836.1, ECO:0000313|Proteomes:UP000294480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 102852 {ECO:0000313|EMBL:TDR30836.1,
RC ECO:0000313|Proteomes:UP000294480};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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: 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:TDR30836.1}.
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DR EMBL; SNZE01000016; TDR30836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R6Y679; -.
DR OrthoDB; 9768187at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000294480; 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}; 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:UP000294480};
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..58
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 70..91
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 103..120
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 165..183
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 189..205
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 212..233
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 291..316
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 328..347
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 367..388
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
SQ SEQUENCE 403 AA; 44215 MW; 27E1155B25010670 CRC64;
MKRFKFRTAG VQTQHDGVPN FLRAPSLARQ EVDWVVLWVP VLLMFLGLVM VYSASIALPD
SNRYKNYSHY AFLIRHAAGI FVGLIVGVFA FRVPTKTWEK LAPLFFVGTL FLLMIVLVVG
RDVGGGRRWL PLGIMNLQPS ELMKIASALY AASYCVRKQG DIRDIGKGVV PMIVVIGIVG
VLLMAEPDLG ALMVIVSIVM GVIFIGGVNY KVFAAIVAIL SAGFAAMVVL TPWRAARLFA
YLDPWTKDNA EGKAYQLTQS LIAFGRGELF GVGLGDSVQK MFYLPEAHTD FILAVIGEEF
GLVGVWAVIL AFTVLVRRSF SIAREAMAFD RVFQSLAVQG IAIWFGVQGF INMGVNMGVL
PTKGLTLPFI SYGGSGILVN CLAIAFILRV DYENRRLMRG ETV
//
