HISP_SALTY
ID HISP_SALTY Reviewed; 258 AA.
AC P02915;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Histidine transport ATP-binding protein HisP;
GN Name=hisP; OrderedLocusNames=STM2351;
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 [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 [3]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=2033074; DOI=10.1016/s0021-9258(18)92898-x;
RA Kerppola R.E., Shyamala V.K., Klebba P., Ames G.F.;
RT "The membrane-bound proteins of periplasmic permeases form a complex.
RT Identification of the histidine permease HisQMP complex.";
RL J. Biol. Chem. 266:9857-9865(1991).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, 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 [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=24021237; DOI=10.1016/j.bbamem.2013.08.024;
RA Heuveling J., Frochaux V., Ziomkowska J., Wawrzinek R., Wessig P.,
RA Herrmann A., Schneider E.;
RT "Conformational changes of the bacterial type I ATP-binding cassette
RT importer HisQMP2 at distinct steps of the catalytic cycle.";
RL Biochim. Biophys. Acta 1838:106-116(2014).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 5-262.
RX PubMed=9872322; DOI=10.1038/25393;
RA Hung L.W., Wang I.X., Nikaido K., Liu P.Q., Ames G.F.-L., Kim S.H.;
RT "Crystal structure of the ATP-binding subunit of an ABC transporter.";
RL Nature 396:703-707(1998).
CC -!- FUNCTION: Part of the histidine permease ABC transporter. Also part of
CC a lysine/arginine/ornithine transporter. Responsible for energy
CC coupling to the transport system. {ECO:0000269|PubMed:24021237,
CC ECO:0000269|PubMed:7050725, ECO:0000269|PubMed:9520394}.
CC -!- ACTIVITY REGULATION: ATPase activity is slightly increased in the
CC presence of HisM and HisQ, and strongly increased when HisJ is also
CC present. {ECO:0000269|PubMed:9520394}.
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 or ArgT). {ECO:0000269|PubMed:2033074,
CC ECO:0000269|PubMed:24021237, ECO:0000269|PubMed:7050725,
CC ECO:0000269|PubMed:9520394}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2033074};
CC Peripheral membrane protein {ECO:0000269|PubMed:2033074}. Note=Binds
CC much more tightly to the membrane in the presence of HisQ and HisM.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; V01373; CAA24662.1; -; Genomic_DNA.
DR EMBL; J01805; AAA75581.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21252.1; -; Genomic_DNA.
DR PIR; A03412; QREBPT.
DR RefSeq; NP_461293.1; NC_003197.2.
DR RefSeq; WP_000986775.1; NC_003197.2.
DR PDB; 1B0U; X-ray; 1.50 A; A=1-258.
DR PDBsum; 1B0U; -.
DR AlphaFoldDB; P02915; -.
DR SMR; P02915; -.
DR STRING; 99287.STM2351; -.
DR TCDB; 3.A.1.3.1; the atp-binding cassette (abc) superfamily.
DR PaxDb; P02915; -.
DR PRIDE; P02915; -.
DR EnsemblBacteria; AAL21252; AAL21252; STM2351.
DR GeneID; 1253873; -.
DR KEGG; stm:STM2351; -.
DR PATRIC; fig|99287.12.peg.2488; -.
DR HOGENOM; CLU_000604_1_22_6; -.
DR OMA; EVFCLIG; -.
DR PhylomeDB; P02915; -.
DR BioCyc; SENT99287:STM2351-MON; -.
DR EvolutionaryTrace; P02915; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015424; F:ABC-type amino acid transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR030679; ABC_ATPase_HisP-typ.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR PIRSF; PIRSF039085; ABC_ATPase_HisP; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; ATP-binding; Cell inner membrane;
KW Cell membrane; Membrane; Nucleotide-binding; Reference proteome; Transport.
FT CHAIN 1..258
FT /note="Histidine transport ATP-binding protein HisP"
FT /id="PRO_0000092342"
FT DOMAIN 7..253
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:1B0U"
FT STRAND 19..29
FT /evidence="ECO:0007829|PDB:1B0U"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:1B0U"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:1B0U"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:1B0U"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1B0U"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:1B0U"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:1B0U"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1B0U"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:1B0U"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:1B0U"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:1B0U"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:1B0U"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:1B0U"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:1B0U"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:1B0U"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:1B0U"
FT HELIX 189..201
FT /evidence="ECO:0007829|PDB:1B0U"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:1B0U"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:1B0U"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:1B0U"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:1B0U"
FT HELIX 237..242
FT /evidence="ECO:0007829|PDB:1B0U"
FT HELIX 247..258
FT /evidence="ECO:0007829|PDB:1B0U"
SQ SEQUENCE 258 AA; 28771 MW; D7646F4DA43C62F8 CRC64;
MMSENKLHVI DLHKRYGGHE VLKGVSLQAR AGDVISIIGS SGSGKSTFLR CINFLEKPSE
GAIIVNGQNI NLVRDKDGQL KVADKNQLRL LRTRLTMVFQ HFNLWSHMTV LENVMEAPIQ
VLGLSKHDAR ERALKYLAKV GIDERAQGKY PVHLSGGQQQ RVSIARALAM EPDVLLFDEP
TSALDPELVG EVLRIMQQLA EEGKTMVVVT HEMGFARHVS SHVIFLHQGK IEEEGDPEQV
FGNPQSPRLQ QFLKGSLK
