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Database: UniProt
Entry: Q0FT07_SALBH
LinkDB: Q0FT07_SALBH
Original site: Q0FT07_SALBH 
ID   Q0FT07_SALBH            Unreviewed;       386 AA.
AC   Q0FT07;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 58.
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=R2601_21161 {ECO:0000313|EMBL:EAU47362.1};
OS   Salipiger bermudensis (strain DSM 26914 / JCM 13377 / KCTC 12554 /
OS   HTCC2601) (Pelagibaca bermudensis).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=314265 {ECO:0000313|EMBL:EAU47362.1, ECO:0000313|Proteomes:UP000006230};
RN   [1] {ECO:0000313|EMBL:EAU47362.1, ECO:0000313|Proteomes:UP000006230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26914 / JCM 13377 / KCTC 12554 / HTCC2601
RC   {ECO:0000313|Proteomes:UP000006230};
RX   PubMed=20729358; DOI=10.1128/JB.00873-10;
RA   Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT   alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT   genera.";
RL   J. Bacteriol. 192:5552-5553(2010).
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}.
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:EAU47362.1}.
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DR   EMBL; AATQ01000007; EAU47362.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0FT07; -.
DR   STRING; 314265.R2601_21161; -.
DR   eggNOG; COG0772; Bacteria.
DR   HOGENOM; CLU_029243_1_1_5; -.
DR   Proteomes; UP000006230; Unassembled WGS sequence.
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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000313|EMBL:EAU47362.1};
KW   Cell division {ECO:0000313|EMBL:EAU47362.1};
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:UP000006230};
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        26..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        188..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        281..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        314..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        347..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   386 AA;  41403 MW;  9C91B19B82CB1F35 CRC64;
     MVYGTVSSVR EGEPVLPKWW RTVDRWALSC ILMLFGVGIL LGLAASPPLA ERNGFGHFHY
     VQRQAFFGGL ALTAMLLTSM MTPVQVRRIA VIGFLGAFIA LLGLPFLGTD FGKGAVRWYS
     LGFASVQPSE FLKPLFVIVV AWLMAASQEI GGPPGKLWSF GLTVTIVLTL ALQPDFGQAC
     LVLFGWGVMW FVAGAPMLLL VGLAALVVLG GMVAYNNSEH FARRIDGFLT PEVDPTTQLG
     YATNAIQEGG FFGVGVGEGT VKWSLPDAHT DFIIAVAAEE YGLILVLAII ALYTTVVVRS
     MMRLIRERDP FIRLAGTGLA AMFGVQAMIN MGVAVRLLPA KGMTLPFVSY GGSSLIAGGI
     ALGMLLAFTR TRPQGEIGEI LRGRAR
//
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