ID HISJ_ECOLI Reviewed; 260 AA.
AC P0AEU0; P39182; P77763;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Histidine-binding periplasmic protein {ECO:0000305};
DE Short=HBP;
DE Flags: Precursor;
GN Name=hisJ; OrderedLocusNames=b2309, JW2306;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Joshi A., Ames G.F.-L.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 23-40.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP PROTEIN SEQUENCE OF 23-26.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [7] {ECO:0007744|PDB:1HSL}
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH HISTIDINE, DISULFIDE
RP BOND, AND DOMAIN.
RC STRAIN=K12;
RX PubMed=8161536; DOI=10.1021/bi00182a004;
RA Yao N., Trakhanov S., Quiocho F.A.;
RT "Refined 1.89-A structure of the histidine-binding protein complexed with
RT histidine and its relationship with many other active
RT transport/chemosensory proteins.";
RL Biochemistry 33:4769-4779(1994).
CC -!- FUNCTION: Part of the ABC transporter complex HisPMQJ involved in
CC histidine transport (By similarity). Binds histidine (By similarity).
CC Interacts with HisQMP and stimulates ATPase activity of HisP, which
CC results in histidine translocation (By similarity).
CC {ECO:0000250|UniProtKB:P02910}.
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|UniProtKB:P02910}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P02910}.
CC -!- DOMAIN: Has a bi-lobal structure (PubMed:8161536). Contains two similar
CC globular domains separated by a deep cleft wherein the ligand-binding
CC site is located (PubMed:8161536). {ECO:0000269|PubMed:8161536}.
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; U47027; AAA85769.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75369.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16155.1; -; Genomic_DNA.
DR PIR; C65003; C65003.
DR RefSeq; NP_416812.1; NC_000913.3.
DR RefSeq; WP_000737621.1; NZ_STEB01000008.1.
DR PDB; 1HSL; X-ray; 1.89 A; A/B=23-260.
DR PDBsum; 1HSL; -.
DR AlphaFoldDB; P0AEU0; -.
DR BMRB; P0AEU0; -.
DR SASBDB; P0AEU0; -.
DR SMR; P0AEU0; -.
DR BioGRID; 4260524; 15.
DR ComplexPortal; CPX-4328; Histidine ABC transporter complex.
DR DIP; DIP-9908N; -.
DR IntAct; P0AEU0; 7.
DR STRING; 511145.b2309; -.
DR BindingDB; P0AEU0; -.
DR TCDB; 3.A.1.3.29; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P0AEU0; -.
DR jPOST; P0AEU0; -.
DR PaxDb; 511145-b2309; -.
DR EnsemblBacteria; AAC75369; AAC75369; b2309.
DR GeneID; 83580101; -.
DR GeneID; 945309; -.
DR KEGG; ecj:JW2306; -.
DR KEGG; eco:b2309; -.
DR PATRIC; fig|511145.12.peg.2404; -.
DR EchoBASE; EB2045; -.
DR eggNOG; COG0834; Bacteria.
DR HOGENOM; CLU_019602_18_0_6; -.
DR InParanoid; P0AEU0; -.
DR OMA; GACCKIL; -.
DR OrthoDB; 9768183at2; -.
DR PhylomeDB; P0AEU0; -.
DR BioCyc; EcoCyc:HISJ-MONOMER; -.
DR EvolutionaryTrace; P0AEU0; -.
DR PRO; PR:P0AEU0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; NAS:ComplexPortal.
DR GO; GO:0016020; C:membrane; NAS:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0016597; F:amino acid binding; IDA:EcoCyc.
DR GO; GO:1903810; P:L-histidine import across plasma membrane; NAS:ComplexPortal.
DR CDD; cd13703; PBP2_HisJ_LAO; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR005768; Lys_Arg_Orn-bd.
DR InterPro; IPR018313; SBP_3_CS.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR NCBIfam; TIGR01096; 3A0103s03R; 1.
DR PANTHER; PTHR35936:SF13; HISTIDINE-BINDING PERIPLASMIC PROTEIN; 1.
DR PANTHER; PTHR35936; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR SMART; SM00062; PBPb; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 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:9298646,
FT ECO:0000269|PubMed:9600841"
FT CHAIN 23..260
FT /note="Histidine-binding periplasmic protein"
FT /id="PRO_0000031762"
FT BINDING 91
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000269|PubMed:8161536,
FT ECO:0007744|PDB:1HSL"
FT BINDING 92
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000269|PubMed:8161536,
FT ECO:0007744|PDB:1HSL"
FT BINDING 94
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000269|PubMed:8161536,
FT ECO:0007744|PDB:1HSL"
FT BINDING 99
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000269|PubMed:8161536,
FT ECO:0007744|PDB:1HSL"
FT BINDING 143
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000269|PubMed:8161536,
FT ECO:0007744|PDB:1HSL"
FT BINDING 183
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000269|PubMed:8161536,
FT ECO:0007744|PDB:1HSL"
FT DISULFID 60..67
FT /evidence="ECO:0000269|PubMed:8161536,
FT ECO:0007744|PDB:1HSL"
FT CONFLICT 21
FT /note="F -> L (in Ref. 1; AAA85769)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="S -> G (in Ref. 1; AAA85769)"
FT /evidence="ECO:0000305"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1HSL"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:1HSL"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1HSL"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1HSL"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:1HSL"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1HSL"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:1HSL"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1HSL"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:1HSL"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1HSL"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:1HSL"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:1HSL"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1HSL"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:1HSL"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1HSL"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:1HSL"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:1HSL"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:1HSL"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:1HSL"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:1HSL"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:1HSL"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:1HSL"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:1HSL"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1HSL"
FT HELIX 226..241
FT /evidence="ECO:0007829|PDB:1HSL"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:1HSL"
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
//
