MNTH_ECOLI
ID MNTH_ECOLI Reviewed; 412 AA.
AC P0A769; P77145;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Divalent metal cation transporter MntH {ECO:0000255|HAMAP-Rule:MF_00221};
GN Name=mntH {ECO:0000255|HAMAP-Rule:MF_00221}; Synonyms=yfeP;
GN OrderedLocusNames=b2392, JW2388;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12 / MM1955;
RX PubMed=10844693; DOI=10.1046/j.1365-2958.2000.01922.x;
RA Kehres D.G., Zaharik M.L., Finlay B.B., Maguire M.E.;
RT "The NRAMP proteins of Salmonella typhimurium and Escherichia coli are
RT selective manganese transporters involved in the response to reactive
RT oxygen.";
RL Mol. Microbiol. 36:1085-1100(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=10712688; DOI=10.1046/j.1365-2958.2000.01774.x;
RA Makui H., Roig E., Cole S.T., Helmann J.D., Gros P., Cellier M.F.M.;
RT "Identification of the Escherichia coli K-12 Nramp orthologue (MntH) as a
RT selective divalent metal ion transporter.";
RL Mol. Microbiol. 35:1065-1078(2000).
RN [6]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=14607838; DOI=10.1074/jbc.m309913200;
RA Courville P., Chaloupka R., Veyrier F., Cellier M.F.M.;
RT "Determination of transmembrane topology of the Escherichia coli natural
RT resistance-associated macrophage protein (Nramp) ortholog.";
RL J. Biol. Chem. 279:3318-3326(2004).
RN [7]
RP MUTAGENESIS OF ASP-34; PRO-35; GLY-36; ASN-37; GLU-102; ASP-109; GLU-112;
RP GLY-115; GLU-154 AND ASP-238.
RX PubMed=15630547; DOI=10.1007/s00232-004-0711-x;
RA Haemig H.A., Brooker R.J.;
RT "Importance of conserved acidic residues in mntH, the Nramp homolog of
RT Escherichia coli.";
RL J. Membr. Biol. 201:97-107(2004).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: H(+)-stimulated, divalent metal cation uptake system.
CC Involved in manganese and iron uptake. Can also transport cadmium,
CC cobalt, zinc and to a lesser extent nickel and copper. Involved in
CC response to reactive oxygen. {ECO:0000255|HAMAP-Rule:MF_00221,
CC ECO:0000269|PubMed:10712688, ECO:0000269|PubMed:10844693}.
CC -!- INTERACTION:
CC P0A769; P09372: grpE; NbExp=3; IntAct=EBI-551337, EBI-547441;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00221, ECO:0000269|PubMed:14607838}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00221, ECO:0000269|PubMed:14607838}.
CC -!- SIMILARITY: Belongs to the NRAMP family. {ECO:0000255|HAMAP-
CC Rule:MF_00221}.
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DR EMBL; AF161318; AAD46617.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75451.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16262.1; -; Genomic_DNA.
DR PIR; E65013; E65013.
DR RefSeq; NP_416893.1; NC_000913.3.
DR RefSeq; WP_000186369.1; NZ_STEB01000008.1.
DR AlphaFoldDB; P0A769; -.
DR SMR; P0A769; -.
DR BioGRID; 4259183; 8.
DR DIP; DIP-48004N; -.
DR IntAct; P0A769; 1.
DR STRING; 511145.b2392; -.
DR TCDB; 2.A.55.3.1; the metal ion (mn(2+)-iron) transporter (nramp) family.
DR PaxDb; P0A769; -.
DR PRIDE; P0A769; -.
DR EnsemblBacteria; AAC75451; AAC75451; b2392.
DR EnsemblBacteria; BAA16262; BAA16262; BAA16262.
DR GeneID; 66673738; -.
DR GeneID; 946899; -.
DR KEGG; ecj:JW2388; -.
DR KEGG; eco:b2392; -.
DR PATRIC; fig|1411691.4.peg.4337; -.
DR EchoBASE; EB3909; -.
DR eggNOG; COG1914; Bacteria.
DR HOGENOM; CLU_020088_2_0_6; -.
DR InParanoid; P0A769; -.
DR OMA; IATFVNS; -.
DR PhylomeDB; P0A769; -.
DR BioCyc; EcoCyc:YFEP-MON; -.
DR BioCyc; MetaCyc:YFEP-MON; -.
DR PRO; PR:P0A769; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IMP:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoliWiki.
DR GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IMP:EcoliWiki.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IMP:EcoliWiki.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IMP:EcoliWiki.
DR GO; GO:0015293; F:symporter activity; IDA:EcoliWiki.
DR GO; GO:0015292; F:uniporter activity; IMP:EcoliWiki.
DR GO; GO:0015691; P:cadmium ion transport; IDA:EcoliWiki.
DR GO; GO:0071281; P:cellular response to iron ion; IBA:GO_Central.
DR GO; GO:0006824; P:cobalt ion transport; IMP:EcoliWiki.
DR GO; GO:0006826; P:iron ion transport; IMP:EcoliWiki.
DR GO; GO:0006828; P:manganese ion transport; IMP:EcoCyc.
DR GO; GO:0030001; P:metal ion transport; IMP:EcoliWiki.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Ion transport; Iron; Manganese;
KW Membrane; Reference proteome; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..412
FT /note="Divalent metal cation transporter MntH"
FT /id="PRO_0000212617"
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"
FT MUTAGEN 34
FT /note="D->E,N: Loss of function."
FT /evidence="ECO:0000269|PubMed:15630547"
FT MUTAGEN 35
FT /note="P->N,Q: Loss of function."
FT /evidence="ECO:0000269|PubMed:15630547"
FT MUTAGEN 36
FT /note="G->P: Loss of function."
FT /evidence="ECO:0000269|PubMed:15630547"
FT MUTAGEN 37
FT /note="N->D: Loss of function."
FT /evidence="ECO:0000269|PubMed:15630547"
FT MUTAGEN 102
FT /note="E->D,Q: Loss of function."
FT /evidence="ECO:0000269|PubMed:15630547"
FT MUTAGEN 109
FT /note="D->E,N: Transports manganese to a very low level."
FT /evidence="ECO:0000269|PubMed:15630547"
FT MUTAGEN 112
FT /note="E->D,Q: Transports manganese to a very low level."
FT /evidence="ECO:0000269|PubMed:15630547"
FT MUTAGEN 115
FT /note="G->A,P: Loss of function."
FT /evidence="ECO:0000269|PubMed:15630547"
FT MUTAGEN 154
FT /note="E->Q: Transports manganese to a level half of that
FT of wild-type."
FT /evidence="ECO:0000269|PubMed:15630547"
FT MUTAGEN 238
FT /note="D->N: Transports manganese to a very low level."
FT /evidence="ECO:0000269|PubMed:15630547"
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
