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HISM_SALTY
ID   HISM_SALTY              Reviewed;         235 AA.
AC   P0A2I7; P02912;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Histidine transport system permease protein HisM;
GN   Name=hisM; OrderedLocusNames=STM2352;
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   TOPOLOGY.
RX   PubMed=1733937; DOI=10.1016/s0021-9258(18)45882-6;
RA   Kerppola R.E., Ames G.F.-L.;
RT   "Topology of the hydrophobic membrane-bound components of the histidine
RT   periplasmic permease. Comparison with other members of the family.";
RL   J. Biol. Chem. 267:2329-2336(1992).
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 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).
CC   -!- FUNCTION: Part of the histidine permease ABC transporter. Also part of
CC       a lysine/arginine/ornithine transporter. Probably responsible for the
CC       translocation of the substrate across the membrane. Required to relay
CC       the ATPase-inducing signal from the solute-binding protein to HisP.
CC       {ECO:0000269|PubMed:24021237, ECO:0000269|PubMed:7050725,
CC       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       Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
CC       ECO:0000269|PubMed:2033074}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. HisMQ subfamily. {ECO:0000305}.
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DR   EMBL; V01373; CAA24661.1; -; Genomic_DNA.
DR   EMBL; J01805; AAA75580.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL21253.1; -; Genomic_DNA.
DR   PIR; A03409; MMEBMT.
DR   RefSeq; NP_461294.1; NC_003197.2.
DR   RefSeq; WP_000569771.1; NC_003197.2.
DR   AlphaFoldDB; P0A2I7; -.
DR   SMR; P0A2I7; -.
DR   STRING; 99287.STM2352; -.
DR   TCDB; 3.A.1.3.1; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P0A2I7; -.
DR   EnsemblBacteria; AAL21253; AAL21253; STM2352.
DR   GeneID; 1253874; -.
DR   KEGG; stm:STM2352; -.
DR   PATRIC; fig|99287.12.peg.2489; -.
DR   HOGENOM; CLU_019602_1_4_6; -.
DR   OMA; FFQNAWY; -.
DR   PhylomeDB; P0A2I7; -.
DR   BioCyc; SENT99287:STM2352-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR010065; AA_ABC_transptr_permease_3TM.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   TIGRFAMs; TIGR01726; HEQRo_perm_3TM; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..235
FT                   /note="Histidine transport system permease protein HisM"
FT                   /id="PRO_0000060048"
FT   TOPO_DOM        1..26
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        48..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        80..104
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        126..157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        179..199
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        221..235
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          23..221
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   235 AA;  26453 MW;  225000C96D1818A3 CRC64;
     MIEIIQEYWK SLLWTDGYRF TGVAITLWLL ISSVVMGGLL AVILAVGRVS SNKFIRFPIW
     LFTYIFRGTP LYVQLLVFYS GMYTLEIVKG TDLLNAFFRS GLNCTVLALT LNTCAYTTEI
     FAGAIRSVPH GEIEAARAYG FSSFKMYRCI ILPSALRIAL PAYSNEVILM LHSTALAFTA
     TVPDLLKIAR DINSATYQPF TAFGIAAVLY LLISYVLISL FRRAERRWLQ HVSSK
 
 
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