ID   HISJ_ECOL6              Reviewed;         260 AA.
AC   P0AEU1; P39182; P77763;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Histidine-binding periplasmic protein;
DE            Short=HBP;
DE   Flags: Precursor;
GN   Name=hisJ; OrderedLocusNames=c2851;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Part of the histidine permease ABC transporter. Binds
CC       histidine. Interacts with HisQMP and stimulates ATPase activity of
CC       HisP, which results in histidine translocation (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (HisP),
CC       two transmembrane proteins (HisM and HisQ) and a solute-binding protein
CC       (HisJ). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC       {ECO:0000305}.
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DR   EMBL; AE014075; AAN81305.1; -; Genomic_DNA.
DR   RefSeq; WP_000737621.1; NC_004431.1.
DR   AlphaFoldDB; P0AEU1; -.
DR   BMRB; P0AEU1; -.
DR   SMR; P0AEU1; -.
DR   STRING; 199310.c2851; -.
DR   EnsemblBacteria; AAN81305; AAN81305; c2851.
DR   GeneID; 67416739; -.
DR   KEGG; ecc:c2851; -.
DR   eggNOG; COG0834; Bacteria.
DR   HOGENOM; CLU_019602_18_0_6; -.
DR   OMA; FSEEPYG; -.
DR   BioCyc; ECOL199310:C2851-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005768; Lys_Arg_Orn-bd.
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   TIGRFAMs; TIGR01096; 3A0103s03R; 1.
DR   PROSITE; PS01039; SBP_BACTERIAL_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Disulfide bond; Periplasm; Signal; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..260
FT                   /note="Histidine-binding periplasmic protein"
FT                   /id="PRO_0000045057"
FT   DISULFID        60..67
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   260 AA;  28483 MW;  28BFFD0C67ABF716 CRC64;
     MKKLVLSLSL VLAFSSATAA FAAIPQNIRI GTDPTYAPFE SKNSQGELVG FDIDLAKELC
     KRINTQCTFV ENPLDALIPS LKAKKIDAIM SSLSITEKRQ QEIAFTDKLY AADSRLVVAK
     NSDIQPTVES LKGKRVGVLQ GTTQETFGNE HWAPKGIEIV SYQGQDNIYS DLTAGRIDAA
     FQDEVAASEG FLKQPVGKDY KFGGPSVKDE KLFGVGTGMG LRKEDNELRE ALNKAFAEMR
     ADGTYEKLAK KYFDFDVYGG