ID   HISJ_ECO57              Reviewed;         260 AA.
AC   P0AEU2; P39182; P77763;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Histidine-binding periplasmic protein;
DE            Short=HBP;
DE   Flags: Precursor;
GN   Name=hisJ; OrderedLocusNames=Z3571, ECs3193;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG57438.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36616.1; -; Genomic_DNA.
DR   PIR; A91028; A91028.
DR   PIR; B85872; B85872.
DR   RefSeq; NP_311220.1; NC_002695.1.
DR   RefSeq; WP_000737621.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AEU2; -.
DR   BMRB; P0AEU2; -.
DR   SMR; P0AEU2; -.
DR   STRING; 155864.EDL933_3475; -.
DR   EnsemblBacteria; AAG57438; AAG57438; Z3571.
DR   EnsemblBacteria; BAB36616; BAB36616; ECs_3193.
DR   GeneID; 67416739; -.
DR   GeneID; 916901; -.
DR   KEGG; ece:Z3571; -.
DR   KEGG; ecs:ECs_3193; -.
DR   PATRIC; fig|386585.9.peg.3333; -.
DR   eggNOG; COG0834; Bacteria.
DR   HOGENOM; CLU_019602_18_0_6; -.
DR   OMA; FSEEPYG; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; Reference proteome;
KW   Signal; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..260
FT                   /note="Histidine-binding periplasmic protein"
FT                   /id="PRO_0000045056"
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