MNTH_ECO81
ID MNTH_ECO81 Reviewed; 412 AA.
AC B7MY49;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Divalent metal cation transporter MntH {ECO:0000255|HAMAP-Rule:MF_00221};
GN Name=mntH {ECO:0000255|HAMAP-Rule:MF_00221}; OrderedLocusNames=ECED1_2838;
OS Escherichia coli O81 (strain ED1a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585397;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED1a;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928162; CAR09015.2; -; Genomic_DNA.
DR RefSeq; WP_000186369.1; NC_011745.1.
DR AlphaFoldDB; B7MY49; -.
DR SMR; B7MY49; -.
DR EnsemblBacteria; CAR09015; CAR09015; ECED1_2838.
DR GeneID; 66673738; -.
DR KEGG; ecq:ECED1_2838; -.
DR HOGENOM; CLU_020088_2_0_6; -.
DR OMA; IATFVNS; -.
DR Proteomes; UP000000748; 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..412
FT /note="Divalent metal cation transporter MntH"
FT /id="PRO_1000124865"
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..412
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
SQ SEQUENCE 412 AA; 44194 MW; 7D77FEAEA00411FB CRC64;
MTNYRVESSS GRAARKMRLA LMGPAFIAAI GYIDPGNFAT NIQAGASFGY QLLWVVVWAN
LMAMLIQILS AKLGIATGKN LAEQIRDHYP RPVVWFYWVQ AEIIAMATDL AEFIGAAIGF
KLILGVSLLQ GAVLTGIATF LILMLQRRGQ KPLEKVIGGL LLFVAAAYIV ELIFSQPNLA
QLGKGMVIPS LPTSEAVFLA AGVLGATIMP HVIYLHSSLT QHLHGGSRQQ RYSATKWDVA
IAMTIAGFVN LAMMATAAAA FHFSGHTGVA DLDEAYLTLQ PLLSHAAATV FGLSLVAAGL
SSTVVGTLAG QVVMQGFIRF HIPLWVRRTV TMLPSFIVIL MGLDPTRILV MSQVLLSFGI
ALALVPLLIF TSDSKLMGDL VNSKRVKQTG WVIVVLVVAL NIWLLVGTAL GL
