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Database: UniProt
Entry: A0A4D7CUM7_9ENTE
LinkDB: A0A4D7CUM7_9ENTE
Original site: A0A4D7CUM7_9ENTE 
ID   A0A4D7CUM7_9ENTE        Unreviewed;       389 AA.
AC   A0A4D7CUM7;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Probable peptidoglycan glycosyltransferase FtsW {ECO:0000256|ARBA:ARBA00041185};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE   AltName: Full=Cell division protein FtsW {ECO:0000256|ARBA:ARBA00041418};
DE   AltName: Full=Cell wall polymerase {ECO:0000256|ARBA:ARBA00033270};
DE   AltName: Full=Peptidoglycan polymerase {ECO:0000256|ARBA:ARBA00032370};
GN   ORFNames=FA707_03230 {ECO:0000313|EMBL:QCI86031.1}, FE258_05930
GN   {ECO:0000313|EMBL:TLG80225.1};
OS   Vagococcus zengguangii.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX   NCBI_TaxID=2571750 {ECO:0000313|EMBL:QCI86031.1, ECO:0000313|Proteomes:UP000298615};
RN   [1] {ECO:0000313|EMBL:QCI86031.1, ECO:0000313|Proteomes:UP000298615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MN-17 {ECO:0000313|EMBL:QCI86031.1,
RC   ECO:0000313|Proteomes:UP000298615};
RA   Ge Y.;
RT   "Vagococcus sp. nov., isolated from faeces of yaks (Bos grunniens).";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TLG80225.1, ECO:0000313|Proteomes:UP000306774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MN-09 {ECO:0000313|EMBL:TLG80225.1,
RC   ECO:0000313|Proteomes:UP000306774};
RA   Ge Y.;
RT   "Vagococcus sp. nov., isolated from feces of yaks (Bos grunniens).";
RL   Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily.
CC       {ECO:0000256|ARBA:ARBA00038053}.
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DR   EMBL; CP039712; QCI86031.1; -; Genomic_DNA.
DR   EMBL; VCAP01000006; TLG80225.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4D7CUM7; -.
DR   KEGG; vao:FA707_03230; -.
DR   Proteomes; UP000298615; Chromosome.
DR   Proteomes; UP000306774; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   InterPro; IPR018365; Cell_cycle_FtsW-rel_CS.
DR   InterPro; IPR001182; FtsW/RodA.
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 shape {ECO:0000256|ARBA:ARBA00022960};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000298615};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        46..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        107..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        171..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        199..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        277..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        319..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        349..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   389 AA;  42325 MW;  F75838A0BEE8616C CRC64;
     MVNKPKKRYF LDYGILIPYI ALSIIGVVMV YSATAYRLIN AGANEFSGGI KQAAFFIVGL
     ILIYIIYHMK IDFLRNKRVI NISLAAIIGM LMLTLIIGTA LGGAKGWITV AGVQIQPVEF
     LKIIVIWYLS NVVASRQAEI QRSFTQSFFG PMIAIGISVF LLLLQPDTGG AAIVVLLTLV
     MLLASGISYW YGIAVTGGGV ALSVIAIEFV TLIGKYFLPE YIVNRFLVFR NPFIDPYASG
     MQMIQSYYAM FNGGLFGRGL GNSIQKKGFL PVAESDFIFS IIIEELGLIA AIIILCILLF
     LILRILAVGI SATSTFNSMM CIGISAMMLI QTFINVGGIT GLIPMTGVTF PFISQGGSSF
     IALSIGVGLA LNIRADELRK KHQRHIEAL
//
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