HISM_SALTI
ID HISM_SALTI Reviewed; 235 AA.
AC P0A2I8; P02912;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Histidine transport system permease protein HisM;
GN Name=hisM; OrderedLocusNames=STY2582, t0512;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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 (By
CC similarity). {ECO:0000250}.
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. HisMQ subfamily. {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; AL513382; CAD07584.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68218.1; -; Genomic_DNA.
DR RefSeq; NP_456894.1; NC_003198.1.
DR RefSeq; WP_000569771.1; NZ_WSUR01000029.1.
DR AlphaFoldDB; P0A2I8; -.
DR SMR; P0A2I8; -.
DR STRING; 220341.16503576; -.
DR EnsemblBacteria; AAO68218; AAO68218; t0512.
DR KEGG; stt:t0512; -.
DR KEGG; sty:STY2582; -.
DR PATRIC; fig|220341.7.peg.2614; -.
DR eggNOG; COG4160; Bacteria.
DR HOGENOM; CLU_019602_1_4_6; -.
DR OMA; FFQNAWY; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..235
FT /note="Histidine transport system permease protein HisM"
FT /id="PRO_0000060047"
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
