Y3382_XANCP
ID Y3382_XANCP Reviewed; 314 AA.
AC Q8P5F9;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=DegV domain-containing protein XCC3382;
GN OrderedLocusNames=XCC3382;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
CC -!- FUNCTION: May bind long-chain fatty acids, such as palmitate, and may
CC play a role in lipid transport or fatty acid metabolism. {ECO:0000250}.
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DR EMBL; AE008922; AAM42652.1; -; Genomic_DNA.
DR RefSeq; NP_638728.1; NC_003902.1.
DR RefSeq; WP_011038480.1; NC_003902.1.
DR AlphaFoldDB; Q8P5F9; -.
DR SMR; Q8P5F9; -.
DR STRING; 340.xcc-b100_0817; -.
DR EnsemblBacteria; AAM42652; AAM42652; XCC3382.
DR KEGG; xcc:XCC3382; -.
DR PATRIC; fig|190485.4.peg.3617; -.
DR eggNOG; COG1307; Bacteria.
DR HOGENOM; CLU_069606_0_0_6; -.
DR OMA; HYAESIP; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1180.10; -; 1.
DR InterPro; IPR003797; DegV.
DR InterPro; IPR043168; DegV_C.
DR Pfam; PF02645; DegV; 1.
DR TIGRFAMs; TIGR00762; DegV; 1.
DR PROSITE; PS51482; DEGV; 1.
PE 3: Inferred from homology;
KW Lipid-binding; Reference proteome.
FT CHAIN 1..314
FT /note="DegV domain-containing protein XCC3382"
FT /id="PRO_0000209822"
FT DOMAIN 3..307
FT /note="DegV"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00815"
FT BINDING 63
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250|UniProtKB:Q9X1H9"
FT BINDING 96
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250|UniProtKB:Q9X1H9"
SQ SEQUENCE 314 AA; 34173 MW; 318D007722D5A111 CRC64;
MRIGIVVDSA CDLPQDFIQR NNVIVLPISV RIGEAVLADH RDEEATLSFL HAHVAERGHE
AETTPFSVNQ IRDLFLQRLV IDYDHVFCLT ISKLRSQIFD NATQASFAIL NDYKPVRQAA
GHTSPFALRV IDTLNLFAGQ GITAVEAVRL RAQGLGVAPI RARLEQLAEH TYGYMIPRDL
YYLRARARTK GDRSVGLIGA ALGSALDIKP VLRAYRGVTE PVAKLKGFEP SAEKLFAFTV
RKLREGLMTP TVCVGYGGEL AELHALPGYA ALQAACQTQG VELFESVMSL TGMVNVGKGA
LAVAFAAEPH SFSA