HISJ_SALTY
ID HISJ_SALTY Reviewed; 260 AA.
AC P02910;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Histidine-binding periplasmic protein;
DE Short=HBP;
DE Flags: Precursor;
GN Name=hisJ; OrderedLocusNames=STM2354;
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], FUNCTION, AND SUBUNIT.
RX PubMed=7050725; DOI=10.1038/298723a0;
RA Higgins C.F., Haag P.D., Nikaido K., Ardeshir F., Garcia G., Ames G.F.-L.;
RT "Complete nucleotide sequence and identification of membrane components of
RT the histidine transport operon of S. typhimurium.";
RL Nature 298:723-727(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6273842; DOI=10.1073/pnas.78.10.6038;
RA Higgins C.F., Ames G.F.-L.;
RT "Two periplasmic transport proteins which interact with a common membrane
RT receptor show extensive homology: complete nucleotide sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:6038-6042(1981).
RN [3]
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).
RN [4]
RP PROTEIN SEQUENCE OF 23-260.
RX PubMed=7007375; DOI=10.1016/s0021-9258(19)69897-2;
RA Hogg R.W.;
RT "The amino acid sequence of the histidine binding protein of Salmonella
RT typhimurium.";
RL J. Biol. Chem. 256:1935-1939(1981).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9520394; DOI=10.1073/pnas.95.7.3495;
RA Liu P.Q., Ames G.F.;
RT "In vitro disassembly and reassembly of an ABC transporter, the histidine
RT permease.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:3495-3500(1998).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLU-40; LYS-42; GLU-47; ASP-171; ARG-176 AND
RP ASP-178.
RX PubMed=9873010; DOI=10.1074/jbc.274.2.739;
RA Liu C.E., Liu P.Q., Wolf A., Lin E., Ames G.F.;
RT "Both lobes of the soluble receptor of the periplasmic histidine permease,
RT an ABC transporter (traffic ATPase), interact with the membrane-bound
RT complex. Effect of different ligands and consequences for the mechanism of
RT action.";
RL J. Biol. Chem. 274:739-747(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=8307974; DOI=10.1016/s0021-9258(17)41754-6;
RA Oh B.-H., Kang C.-H., de Vont H., Kim S.-H., Nikaido K., Joshi A.K.,
RA Ames G.F.-L.;
RT "The bacterial periplasmic histidine-binding protein. Structure/function
RT analysis of the ligand-binding site and comparison with related proteins.";
RL J. Biol. Chem. 269:4135-4143(1994).
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. May have some
CC additional function(s) in translocation that is independent of the
CC stimulation of ATP hydrolysis. {ECO:0000269|PubMed:7050725,
CC ECO:0000269|PubMed:9520394, ECO:0000269|PubMed:9873010}.
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:0000269|PubMed:7050725, ECO:0000269|PubMed:9520394}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC {ECO:0000305}.
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; V01373; CAA24659.1; -; Genomic_DNA.
DR EMBL; V01372; CAA24658.1; -; Genomic_DNA.
DR EMBL; J01805; AAA75578.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21255.1; -; Genomic_DNA.
DR PIR; A93893; JHEBT.
DR RefSeq; NP_461296.1; NC_003197.2.
DR RefSeq; WP_000731868.1; NC_003197.2.
DR PDB; 1HPB; X-ray; 2.50 A; P=23-260.
DR PDBsum; 1HPB; -.
DR AlphaFoldDB; P02910; -.
DR BMRB; P02910; -.
DR SMR; P02910; -.
DR STRING; 99287.STM2354; -.
DR PaxDb; P02910; -.
DR EnsemblBacteria; AAL21255; AAL21255; STM2354.
DR GeneID; 1253876; -.
DR KEGG; stm:STM2354; -.
DR PATRIC; fig|99287.12.peg.2491; -.
DR HOGENOM; CLU_019602_18_0_6; -.
DR OMA; FSEEPYG; -.
DR PhylomeDB; P02910; -.
DR BioCyc; SENT99287:STM2354-MON; -.
DR EvolutionaryTrace; P02910; -.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Direct protein sequencing;
KW Disulfide bond; Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:7007375"
FT CHAIN 23..260
FT /note="Histidine-binding periplasmic protein"
FT /id="PRO_0000031763"
FT DISULFID 60..67
FT /evidence="ECO:0000269|PubMed:7007375"
FT MUTAGEN 40
FT /note="E->K: Decrease in ATPase-inducing activity and
FT histidine transport; when associated with K-47."
FT /evidence="ECO:0000269|PubMed:9873010"
FT MUTAGEN 42
FT /note="K->E: Increases ATPase-inducing activity and
FT histidine transport; when associated with K-47."
FT /evidence="ECO:0000269|PubMed:9873010"
FT MUTAGEN 47
FT /note="E->K: Decrease in ATPase-inducing activity and
FT histidine transport; when associated with K-40. Increases
FT ATPase-inducing activity and histidine transport; when
FT associated with E-42."
FT /evidence="ECO:0000269|PubMed:9873010"
FT MUTAGEN 171
FT /note="D->A,N: Strong decrease in ATPase-inducing activity
FT and histidine transport."
FT /evidence="ECO:0000269|PubMed:9873010"
FT MUTAGEN 176
FT /note="R->D,S: Strong decrease in ATPase-inducing activity
FT and histidine transport."
FT /evidence="ECO:0000269|PubMed:9873010"
FT MUTAGEN 178
FT /note="D->A: Slight decrease in ATPase-inducing activity
FT and histidine transport."
FT /evidence="ECO:0000269|PubMed:9873010"
FT CONFLICT 173
FT /note="T -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 28379 MW; 8F04D7A3DB4F222C CRC64;
MKKLALSLSL VLAFSSATAA FAAIPQKIRI GTDPTYAPFE SKNAQGELVG FDIDLAKELC
KRINTQCTFV ENPLDALIPS LKAKKIDAIM SSLSITEKRQ QEIAFTDKLY AADSRLVVAK
NSDIQPTVAS LKGKRVGVLQ GTTQETFGNE HWAPKGIEIV SYQGQDNIYS DLTAGRIDAA
FQDEVAASEG FLKQPVGKDY KFGGPAVKDE KLFGVGTGMG LRKEDNELRE ALNKAFAEMR
ADGTYEKLAK KYFDFDVYGG
