MNTH_SALPA
ID MNTH_SALPA Reviewed; 413 AA.
AC Q5PNF0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Divalent metal cation transporter MntH {ECO:0000255|HAMAP-Rule:MF_00221};
GN Name=mntH {ECO:0000255|HAMAP-Rule:MF_00221}; OrderedLocusNames=SPA0452;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
CC -!- FUNCTION: H(+)-stimulated, divalent metal cation uptake system.
CC {ECO:0000255|HAMAP-Rule:MF_00221}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00221}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00221}.
CC -!- SIMILARITY: Belongs to the NRAMP family. {ECO:0000255|HAMAP-
CC Rule:MF_00221}.
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DR EMBL; CP000026; AAV76457.1; -; Genomic_DNA.
DR RefSeq; WP_000131734.1; NC_006511.1.
DR AlphaFoldDB; Q5PNF0; -.
DR SMR; Q5PNF0; -.
DR EnsemblBacteria; AAV76457; AAV76457; SPA0452.
DR KEGG; spt:SPA0452; -.
DR HOGENOM; CLU_020088_2_0_6; -.
DR OMA; IATFVNS; -.
DR Proteomes; UP000008185; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00221; NRAMP; 1.
DR InterPro; IPR001046; NRAMP_fam.
DR PANTHER; PTHR11706; PTHR11706; 1.
DR Pfam; PF01566; Nramp; 1.
DR PRINTS; PR00447; NATRESASSCMP.
DR TIGRFAMs; TIGR01197; nramp; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Ion transport; Membrane; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..413
FT /note="Divalent metal cation transporter MntH"
FT /id="PRO_1000024107"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TOPO_DOM 40..51
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 52..71
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TOPO_DOM 72..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 96..118
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TOPO_DOM 119..125
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 126..145
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TOPO_DOM 146..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 156..175
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TOPO_DOM 176..196
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 197..220
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TOPO_DOM 221..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 239..258
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TOPO_DOM 259..276
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TOPO_DOM 298..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 328..344
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TOPO_DOM 345..350
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 351..370
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TOPO_DOM 371..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 388..406
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TOPO_DOM 407..413
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
SQ SEQUENCE 413 AA; 44414 MW; 8BCEC003C0F9F3C3 CRC64;
MTDNRVENSS GRAARKLRLA LMGPAFIAAI GYIDPGNFAT NIQAGASFGY QLLWVVVWAN
LMAMLIQILS AKLGIATGKN LAEQIRDHYP RPVVWFYWVQ AEIIAMATDL AEFIGAAIGF
KLILGVSLLQ GAVLTGIATF LILMLQRRGQ KPLEKVIGGL LLFVAAAYIV ELFFSQPDMA
QLGKGMVIPA LPNPEAVFLA AGVLGATIMP HVIYLHSSLT QHLHGGTRQQ RYSATKWDVA
IAMTIAGFVN LAMMATAAAA FHFSGHTGIA DLDQAYLTLE PLLSHAAATV FGLSLVAAGL
SSTVVGTLAG QVVMQGFVRF HIPLWVRRTI TMLPSFIVIL MGLDPTRILV MSQVLLSFGI
ALALVPLLIF TSNATLMGEL VNTRRVKQIG WIIVVLVVAL NIWLLVGTVM GLS
