MNTH_CLOAB
ID MNTH_CLOAB Reviewed; 431 AA.
AC Q97TN5;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Divalent metal cation transporter MntH {ECO:0000255|HAMAP-Rule:MF_00221};
GN Name=mntH {ECO:0000255|HAMAP-Rule:MF_00221}; OrderedLocusNames=CA_P0063;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OG Plasmid pSOL1.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
CC -!- FUNCTION: H(+)-stimulated, divalent metal cation uptake system.
CC {ECO:0000255|HAMAP-Rule:MF_00221}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00221};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00221}.
CC -!- SIMILARITY: Belongs to the NRAMP family. {ECO:0000255|HAMAP-
CC Rule:MF_00221}.
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DR EMBL; AE001438; AAK76809.1; -; Genomic_DNA.
DR RefSeq; NP_149227.1; NC_001988.2.
DR RefSeq; WP_010890748.1; NC_001988.2.
DR AlphaFoldDB; Q97TN5; -.
DR SMR; Q97TN5; -.
DR EnsemblBacteria; AAK76809; AAK76809; CA_P0063.
DR GeneID; 45000295; -.
DR KEGG; cac:CA_P0063; -.
DR PATRIC; fig|272562.8.peg.63; -.
DR HOGENOM; CLU_020088_2_0_9; -.
DR OMA; IATFVNS; -.
DR OrthoDB; 416257at2; -.
DR Proteomes; UP000000814; Plasmid pSOL1.
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 membrane; Ion transport; Membrane; Plasmid; Reference proteome;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..431
FT /note="Divalent metal cation transporter MntH"
FT /id="PRO_0000212615"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
SQ SEQUENCE 431 AA; 47026 MW; C44D77DDFD5028E9 CRC64;
MDKLSIREDN YNIKHKTISL NRASSVTRNL KGLLKFLGPA FVVSVAYIDP GNFATNISGG
SSFNYNLIWV ILWSNLMAIF LQTMSAKLGI ATGCSLPEMC AKVFSKRANW IFWIVGELGA
MATDLAEFIG GTLGLYLLFR IPMIYAGLLT GVLTFIIVYM EKYGQKMVET IIAALIAVIC
VAYTIELFLA RPAWTQVGMH TLIPSLPNGE AVLIAVGMLG ATVMPHVIYL HSELVQHRNT
NSSDKEKLHH LKMEKIDILI AMNIAFVVNA AMVIVSAAVF FKHGIKVSTI EEAHRSLQPL
LGNLSSGAFG IALLASGLSS SAVGTMAGQT IMKGFVNLSI PINLRRIITM LPALIIIALG
INPMRVLVLS QVALSFILPF PIIQMLLIAG RKDLMGILVN KKFTKIVGFI IATMIILLNI
ILLYLTFTGQ T