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Protein

Histidine-binding periplasmic protein

Gene

hisJ

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Part of the histidine permease ABC transporter. Binds histidine. Interacts with HisQMP and stimulates ATPase activity of HisP, which results in histidine translocation. May have some additional function(s) in translocation that is independent of the stimulation of ATP hydrolysis.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Amino-acid transport, Transport

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-2433-MONOMER.
SENT99287:GCTI-2369-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine-binding periplasmic protein
Short name:
HBP
Gene namesi
Name:hisJ
Ordered Locus Names:STM2354
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401E → K: Decrease in ATPase-inducing activity and histidine transport; when associated with K-47. 1 Publication
Mutagenesisi42 – 421K → E: Increases ATPase-inducing activity and histidine transport; when associated with K-47. 1 Publication
Mutagenesisi47 – 471E → K: Decrease in ATPase-inducing activity and histidine transport; when associated with K-40. Increases ATPase-inducing activity and histidine transport; when associated with E-42. 1 Publication
Mutagenesisi171 – 1711D → A or N: Strong decrease in ATPase-inducing activity and histidine transport. 1 Publication
Mutagenesisi176 – 1761R → D or S: Strong decrease in ATPase-inducing activity and histidine transport. 1 Publication
Mutagenesisi178 – 1781D → A: Slight decrease in ATPase-inducing activity and histidine transport. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 260238Histidine-binding periplasmic proteinPRO_0000031763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi60 ↔ 671 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP02910.
PRIDEiP02910.

Interactioni

Subunit structurei

The complex is composed of two ATP-binding proteins (HisP), two transmembrane proteins (HisM and HisQ) and a solute-binding protein (HisJ).2 Publications

Protein-protein interaction databases

STRINGi99287.STM2354.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HPBX-ray2.50P23-260[»]
ProteinModelPortaliP02910.
SMRiP02910. Positions 23-260.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02910.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105E89. Bacteria.
COG0834. LUCA.
HOGENOMiHOG000031896.
KOiK10014.
OMAiIPYQNQD.
OrthoDBiEOG62VNJH.
PhylomeDBiP02910.

Family and domain databases

InterProiIPR005768. Lys_Arg_Orn-bd.
IPR018313. SBP_3_CS.
IPR001638. Solute-binding_3/MltF_N.
[Graphical view]
PfamiPF00497. SBP_bac_3. 1 hit.
[Graphical view]
SMARTiSM00062. PBPb. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01096. 3A0103s03R. 1 hit.
PROSITEiPS01039. SBP_BACTERIAL_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02910-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKLALSLSL VLAFSSATAA FAAIPQKIRI GTDPTYAPFE SKNAQGELVG
60 70 80 90 100
FDIDLAKELC KRINTQCTFV ENPLDALIPS LKAKKIDAIM SSLSITEKRQ
110 120 130 140 150
QEIAFTDKLY AADSRLVVAK NSDIQPTVAS LKGKRVGVLQ GTTQETFGNE
160 170 180 190 200
HWAPKGIEIV SYQGQDNIYS DLTAGRIDAA FQDEVAASEG FLKQPVGKDY
210 220 230 240 250
KFGGPAVKDE KLFGVGTGMG LRKEDNELRE ALNKAFAEMR ADGTYEKLAK
260
KYFDFDVYGG
Length:260
Mass (Da):28,379
Last modified:July 21, 1986 - v1
Checksum:i8F04D7A3DB4F222C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731T → N AA sequence (PubMed:7007375).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01373 Genomic DNA. Translation: CAA24659.1.
V01372 Genomic DNA. Translation: CAA24658.1.
J01805 Genomic DNA. Translation: AAA75578.1.
AE006468 Genomic DNA. Translation: AAL21255.1.
PIRiA93893. JHEBT.
RefSeqiNP_461296.1. NC_003197.1.
WP_000731868.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL21255; AAL21255; STM2354.
GeneIDi1253876.
KEGGistm:STM2354.
PATRICi32383323. VBISalEnt20916_2491.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01373 Genomic DNA. Translation: CAA24659.1.
V01372 Genomic DNA. Translation: CAA24658.1.
J01805 Genomic DNA. Translation: AAA75578.1.
AE006468 Genomic DNA. Translation: AAL21255.1.
PIRiA93893. JHEBT.
RefSeqiNP_461296.1. NC_003197.1.
WP_000731868.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HPBX-ray2.50P23-260[»]
ProteinModelPortaliP02910.
SMRiP02910. Positions 23-260.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM2354.

Proteomic databases

PaxDbiP02910.
PRIDEiP02910.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL21255; AAL21255; STM2354.
GeneIDi1253876.
KEGGistm:STM2354.
PATRICi32383323. VBISalEnt20916_2491.

Phylogenomic databases

eggNOGiENOG4105E89. Bacteria.
COG0834. LUCA.
HOGENOMiHOG000031896.
KOiK10014.
OMAiIPYQNQD.
OrthoDBiEOG62VNJH.
PhylomeDBiP02910.

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-2433-MONOMER.
SENT99287:GCTI-2369-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP02910.

Family and domain databases

InterProiIPR005768. Lys_Arg_Orn-bd.
IPR018313. SBP_3_CS.
IPR001638. Solute-binding_3/MltF_N.
[Graphical view]
PfamiPF00497. SBP_bac_3. 1 hit.
[Graphical view]
SMARTiSM00062. PBPb. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01096. 3A0103s03R. 1 hit.
PROSITEiPS01039. SBP_BACTERIAL_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete nucleotide sequence and identification of membrane components of the histidine transport operon of S. typhimurium."
    Higgins C.F., Haag P.D., Nikaido K., Ardeshir F., Garcia G., Ames G.F.-L.
    Nature 298:723-727(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT.
  2. "Two periplasmic transport proteins which interact with a common membrane receptor show extensive homology: complete nucleotide sequences."
    Higgins C.F., Ames G.F.-L.
    Proc. Natl. Acad. Sci. U.S.A. 78:6038-6042(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  4. "The amino acid sequence of the histidine binding protein of Salmonella typhimurium."
    Hogg R.W.
    J. Biol. Chem. 256:1935-1939(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-260.
  5. "In vitro disassembly and reassembly of an ABC transporter, the histidine permease."
    Liu P.Q., Ames G.F.
    Proc. Natl. Acad. Sci. U.S.A. 95:3495-3500(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  6. "Both lobes of the soluble receptor of the periplasmic histidine permease, an ABC transporter (traffic ATPase), interact with the membrane-bound complex. Effect of different ligands and consequences for the mechanism of action."
    Liu C.E., Liu P.Q., Wolf A., Lin E., Ames G.F.
    J. Biol. Chem. 274:739-747(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-40; LYS-42; GLU-47; ASP-171; ARG-176 AND ASP-178.
  7. "The bacterial periplasmic histidine-binding protein. Structure/function analysis of the ligand-binding site and comparison with related proteins."
    Oh B.-H., Kang C.-H., de Vont H., Kim S.-H., Nikaido K., Joshi A.K., Ames G.F.-L.
    J. Biol. Chem. 269:4135-4143(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Entry informationi

Entry nameiHISJ_SALTY
AccessioniPrimary (citable) accession number: P02910
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 20, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.