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Database: UniProt
Entry: A0A3D8IW53_9HELI
LinkDB: A0A3D8IW53_9HELI
Original site: A0A3D8IW53_9HELI 
ID   A0A3D8IW53_9HELI        Unreviewed;       385 AA.
AC   A0A3D8IW53;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
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   Name=ftsW {ECO:0000313|EMBL:VEJ24072.1};
GN   ORFNames=CQA62_02395 {ECO:0000313|EMBL:RDU69519.1}, NCTC13205_00199
GN   {ECO:0000313|EMBL:VEJ24072.1};
OS   Helicobacter cholecystus.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=45498 {ECO:0000313|EMBL:RDU69519.1, ECO:0000313|Proteomes:UP000257067};
RN   [1] {ECO:0000313|EMBL:RDU69519.1, ECO:0000313|Proteomes:UP000257067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700242 {ECO:0000313|EMBL:RDU69519.1,
RC   ECO:0000313|Proteomes:UP000257067};
RA   Mannion A.J., Shen Z., Fox J.G.;
RT   "Novel Campyloabacter and Helicobacter Species and Strains.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:VEJ24072.1, ECO:0000313|Proteomes:UP000272814}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13205 {ECO:0000313|EMBL:VEJ24072.1,
RC   ECO:0000313|Proteomes:UP000272814};
RG   Pathogen Informatics;
RL   Submitted (DEC-2018) 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; NXLU01000002; RDU69519.1; -; Genomic_DNA.
DR   EMBL; LR134518; VEJ24072.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8IW53; -.
DR   KEGG; hcl:NCTC13205_00199; -.
DR   OrthoDB; 9768187at2; -.
DR   Proteomes; UP000257067; Unassembled WGS sequence.
DR   Proteomes; UP000272814; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051301; P:cell division; 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 cycle {ECO:0000313|EMBL:RDU69519.1};
KW   Cell division {ECO:0000313|EMBL:RDU69519.1};
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:UP000257067};
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        6..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        43..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        142..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        164..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        187..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        288..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        321..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        355..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   385 AA;  42441 MW;  D519E9E8281C00CE CRC64;
     MQKTIFYSSV ILLCFGIVMV YSLSTYTVLI YDVRSDHFMS KQCISALVAI LLMWLISQLN
     IDCWFKILKN LLFFLSFFAI LAIPFLPESL ATNAGGAQRW IRLFGFSIAP LEFFKIGFIM
     FLSDNLSRNY KPHPSIKDEL ESLFPILLAI IVGFLCVVWS QNDFGQVAVM SISFCVMLLF
     AGGSKKLLGL FATLALIGFV LIITWASRRV ERIKIWWASA QNVVIDKMPF LSFLKVEDMP
     EPYQIYHAGN AIHHGGWLGS GIGGGVVKLG FLSEVHTDMV LAGIAEEFGF FGILGVLGLF
     LFGVIYPILK IANRVQNQMY SLYCVGIACL LSFAFFINAL GVTGVIPIKG IAVPFLSYGG
     SSLVCVGLAL GIVLAISKKI ARPSA
//
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