GenomeNet

Database: UniProt
Entry: A0A074JVJ6_9RHOB
LinkDB: A0A074JVJ6_9RHOB
Original site: A0A074JVJ6_9RHOB 
ID   A0A074JVJ6_9RHOB        Unreviewed;       388 AA.
AC   A0A074JVJ6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=DT23_03195 {ECO:0000313|EMBL:KEO60509.1};
OS   Thioclava indica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Thioclava.
OX   NCBI_TaxID=1353528 {ECO:0000313|EMBL:KEO60509.1, ECO:0000313|Proteomes:UP000027471};
RN   [1] {ECO:0000313|EMBL:KEO60509.1, ECO:0000313|Proteomes:UP000027471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DT23-4 {ECO:0000313|EMBL:KEO60509.1,
RC   ECO:0000313|Proteomes:UP000027471};
RX   PubMed=25361528; DOI=10.1007/s10482-014-0320-3;
RA   Liu Y., Lai Q., Du J., Xu H., Jiang L., Shao Z.;
RT   "Thioclava indica sp. nov., isolated from surface seawater of the Indian
RT   Ocean.";
RL   Antonie Van Leeuwenhoek 107:297-304(2015).
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:KEO60509.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AUNB01000018; KEO60509.1; -; Genomic_DNA.
DR   RefSeq; WP_038129749.1; NZ_AUNB01000018.1.
DR   AlphaFoldDB; A0A074JVJ6; -.
DR   STRING; 1353528.DT23_03195; -.
DR   eggNOG; COG0772; Bacteria.
DR   OrthoDB; 9768187at2; -.
DR   Proteomes; UP000027471; 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:KEO60509.1};
KW   Cell division {ECO:0000313|EMBL:KEO60509.1};
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:UP000027471};
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        28..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        67..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        91..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        159..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        283..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        316..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        349..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   388 AA;  41450 MW;  CA372D34500355B4 CRC64;
     MTEMAFGTVP VRAGEPVLPK WWRTIDKWAL SAVLILFGVG MLLGLAASVP LAERNGLEQF
     YYVKRQAVFG VVALVIMLGI SMLDPRQIRR LGVIGFAGAF VAVMLLPLLG TDFGKGAVRW
     YSLGFASVQP SEFLKPGFVI ISAWFMAAAH EVGGPPGRAY SFLLTCVIVV ALALQPDFGQ
     ASLVLFAWSV MYFVSGAPIA LLTGIGGLAI TGGFFAYNFS DHFARRIDGF LSTDVDPRTQ
     IGYATNAIQE GGFFGVGVGQ GSVKWSLPDA HTDFIIAVAA EEYGLILVLC IIALYATVVI
     RSMLRLTRER DPFTRIAGTG LACAFGIQAI INMGVAVRLL PAKGMTLPFV SYGGSSVIAS
     GIAVGMLLAL TRTRPQGQIS DILARRGR
//
DBGET integrated database retrieval system