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HISJ_CAMJE
ID   HISJ_CAMJE              Reviewed;         256 AA.
AC   Q46125; Q0PAE5; Q9PPH3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Probable histidine-binding protein;
DE            Short=HBP;
DE   AltName: Full=p29;
DE   Flags: Precursor;
GN   Name=hisJ; Synonyms=cjaC; OrderedLocusNames=Cj0734c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN HISTIDINE TRANSPORT.
RC   STRAIN=M275;
RX   PubMed=8751896; DOI=10.1128/iai.64.9.3537-3543.1996;
RA   Garvis S.G., Puzon G.J., Konkel M.E.;
RT   "Molecular characterization of a Campylobacter jejuni 29-kilodalton
RT   periplasmic binding protein.";
RL   Infect. Immun. 64:3537-3543(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M275;
RX   PubMed=9192026; DOI=10.1007/978-1-4899-1828-4_42;
RA   Garvis S.G., Puzon G.J., Konkel M.E.;
RT   "Cloning, sequencing, and expression of a Campylobacter jejuni periplasmic
RT   binding protein (P29) involved in histidine transport.";
RL   Adv. Exp. Med. Biol. 412:263-264(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=72Dz/92;
RX   PubMed=9395059; DOI=10.1111/j.1574-695x.1997.tb01083.x;
RA   Pawelec D., Rozynek E., Popowski J., Jagusztyn-Krynicka E.K.;
RT   "Cloning and characterization of a Campylobacter jejuni 72Dz/92 gene
RT   encoding a 30 kDa immunopositive protein, component of the ABC transport
RT   system; expression of the gene in avirulent Salmonella typhimurium.";
RL   FEMS Immunol. Med. Microbiol. 19:137-150(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
CC   -!- FUNCTION: Involved in histidine transport.
CC       {ECO:0000269|PubMed:8751896}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}. Note=Periplasmic when expressed in E.coli.
CC       {ECO:0000269|PubMed:8751896}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC       {ECO:0000305}.
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DR   EMBL; U58045; AAC35419.1; -; Genomic_DNA.
DR   EMBL; Y10873; CAA71823.1; -; Genomic_DNA.
DR   EMBL; AL111168; CAL34871.1; -; Genomic_DNA.
DR   PIR; A81345; A81345.
DR   RefSeq; YP_002344152.1; NC_002163.1.
DR   AlphaFoldDB; Q46125; -.
DR   SMR; Q46125; -.
DR   IntAct; Q46125; 16.
DR   PRIDE; Q46125; -.
DR   EnsemblBacteria; CAL34871; CAL34871; Cj0734c.
DR   GeneID; 905052; -.
DR   KEGG; cje:Cj0734c; -.
DR   PATRIC; fig|192222.6.peg.726; -.
DR   HOGENOM; CLU_019602_18_2_7; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR018313; SBP_3_CS.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   SMART; SM00062; PBPb; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS01039; SBP_BACTERIAL_3; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           20..256
FT                   /note="Probable histidine-binding protein"
FT                   /id="PRO_0000031764"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        4..8
FT                   /note="FLTAF -> ILSIA (in Ref. 4; CAL34871)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        12..13
FT                   /note="FT -> LV (in Ref. 4; CAL34871)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        18..38
FT                   /note="VACQNTKTENNASNEANTTLT -> GACSDSKNKESNASVE (in Ref.
FT                   4; CAL34871)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52..55
FT                   /note="FKQD -> YKEN (in Ref. 4; CAL34871)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        66
FT                   /note="I -> V (in Ref. 4; CAL34871)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        76
FT                   /note="E -> K (in Ref. 4; CAL34871)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        93
FT                   /note="S -> A (in Ref. 4; CAL34871)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        228
FT                   /note="D -> N (in Ref. 4; CAL34871)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   256 AA;  28531 MW;  2E3E34DFCB92CB29 CRC64;
     MKKFLTAFLV AFTGLFLVAC QNTKTENNAS NEANTTLTLK VGTAPNYKPF NFKQDSKLTG
     FDTDLIEEIA KKNGIEIVWV ETNFDGLIPA LKSGKIDMIA SAMSATDERR QSVDFTKPYY
     MSKNLYLKLK NNDSLQTKND LEGKKIGVQL GTLQENTAKA IKNAQVQSNK DLNIAVLALK
     NNKIDAIVAD QDTAKGFLAE NPELVSFYQE TDGGEGFSFA FDKNKQKDII EIFNKGIDEA
     KTDGFYDTLI KKYELE
 
 
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