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Database: UniProt
Entry: A0A1J0GIA7_9CLOT
LinkDB: A0A1J0GIA7_9CLOT
Original site: A0A1J0GIA7_9CLOT 
ID   A0A1J0GIA7_9CLOT        Unreviewed;       368 AA.
AC   A0A1J0GIA7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=A7L45_14050 {ECO:0000313|EMBL:APC41114.1};
OS   Clostridium estertheticum subsp. estertheticum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1552 {ECO:0000313|EMBL:APC41114.1, ECO:0000313|Proteomes:UP000182569};
RN   [1] {ECO:0000313|Proteomes:UP000182569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8809 {ECO:0000313|Proteomes:UP000182569};
RX   PubMed=27891116;
RA   Yu Z., Gunn L., Brennan E., Reid R., Wall P.G., Gaora O.P., Hurley D.,
RA   Bolton D., Fanning S.;
RT   "Complete Genome Sequence of Clostridium estertheticum DSM 8809, a Microbe
RT   Identified in Spoiled Vacuum Packed Beef.";
RL   Front. Microbiol. 7:1764-1764(2016).
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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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; CP015756; APC41114.1; -; Genomic_DNA.
DR   RefSeq; WP_071613408.1; NZ_CP015756.1.
DR   AlphaFoldDB; A0A1J0GIA7; -.
DR   STRING; 1552.A7L45_14050; -.
DR   KEGG; ceu:A7L45_14050; -.
DR   OrthoDB; 9812661at2; -.
DR   Proteomes; UP000182569; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; IPR013437; FtsW.
DR   InterPro; IPR001182; FtsW/RodA.
DR   InterPro; IPR013438; SpoVE.
DR   NCBIfam; TIGR02614; ftsW; 1.
DR   NCBIfam; TIGR02615; spoVE; 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};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000182569};
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..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        52..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        264..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        302..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        339..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   368 AA;  39882 MW;  AD9A6E4BC7E78992 CRC64;
     MKKHNSKMGQ IDFILFATIM ILVAIGVVMV YSSSSYIAAF KYNDPEYFLK KQIMWAIVGS
     ILMVVAIKID YHILKRYTGI MMVITILLLL VVLAFPAING AKRWIPLGFA SIQPSEIAKY
     TVVLFMAKSL DKKGERVKEF LKGMCPYLLV SGFYAGLVLL GSNLSIAAVI MIVTVIILFA
     AGAKFLHLFA IGSTLVAAVG ALTIFEPYRL ARLMSFRDPF ADSQGKGYQL VQSLLALGSG
     GITGAGIGQS RQKCLYIPEP QTDFIFAIIG EELGLIGCTV IMLLFVIFIW RGIKTAVTCK
     DMYGTILGIG ITSVIAIQAV INIAVVTGSM PVTGVPLPFI SYGGSALVFN MIAMGILLNI
     SRQTANEN
//
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