位置:首页 > 蛋白库 > RFBI_SALTY
RFBI_SALTY
ID   RFBI_SALTY              Reviewed;         330 AA.
AC   P26395;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Protein RfbI;
GN   Name=rfbI; OrderedLocusNames=STM2093;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=1710759; DOI=10.1111/j.1365-2958.1991.tb00741.x;
RA   Jiang X.-M., Neal B., Santiago F., Lee S.J., Romana L.K., Reeves P.R.;
RT   "Structure and sequence of the rfb (O antigen) gene cluster of Salmonella
RT   serovar typhimurium (strain LT2).";
RL   Mol. Microbiol. 5:695-713(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis.
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; X56793; CAA40119.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20997.1; -; Genomic_DNA.
DR   PIR; S15303; S15303.
DR   RefSeq; NP_461038.1; NC_003197.2.
DR   RefSeq; WP_000018226.1; NC_003197.2.
DR   AlphaFoldDB; P26395; -.
DR   SMR; P26395; -.
DR   STRING; 99287.STM2093; -.
DR   PaxDb; P26395; -.
DR   DNASU; 1253614; -.
DR   EnsemblBacteria; AAL20997; AAL20997; STM2093.
DR   GeneID; 1253614; -.
DR   KEGG; stm:STM2093; -.
DR   PATRIC; fig|99287.12.peg.2215; -.
DR   HOGENOM; CLU_003827_7_0_6; -.
DR   OMA; IGLPYGC; -.
DR   PhylomeDB; P26395; -.
DR   BioCyc; SENT99287:STM2093-MON; -.
DR   UniPathway; UPA00281; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   2Fe-2S; Iron; Iron-sulfur; Lipopolysaccharide biosynthesis; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..330
FT                   /note="Protein RfbI"
FT                   /id="PRO_0000189411"
FT   DOMAIN          3..89
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          94..192
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         37
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         42
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         45
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   330 AA;  36583 MW;  EFC1BEC17A0CC82D CRC64;
     MSHIIKIFPS NIEFSGREDE SILDAALSAG IHLEHSCKAG DCGICESDLL AGEVVDSKGN
     IFGQGDKILT CCCKPKTALE LNAHFFPELA GQTKKIVPCK VNSAVLVSGD VMTLKLRTPP
     TAKIGFLPGQ YINLHYKGVT RSYSIANSDE SNGIELHVRN VPNGQMSSLI FGELQENTLM
     RIEGPCGTFF IRESDRPIIF LAGGTGFAPV KSMVEHLIQG KCRREIYIYW GMQYSKDFYS
     ALPQQWSEQH DNVHYIPVVS GDDAEWGGRK GFVHHAVMDD FDSLEFFDIY ACGSPVMIDA
     SKKDFMMKNL SVEHFYSDAF TASNNIEDNL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024