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MNTH_DEIRA
ID   MNTH_DEIRA              Reviewed;         436 AA.
AC   Q9RTP8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=Divalent metal cation transporter MntH {ECO:0000255|HAMAP-Rule:MF_00221};
GN   Name=mntH {ECO:0000255|HAMAP-Rule:MF_00221}; OrderedLocusNames=DR_1709;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
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; AE000513; AAF11265.1; -; Genomic_DNA.
DR   PIR; G75363; G75363.
DR   RefSeq; NP_295432.1; NC_001263.1.
DR   RefSeq; WP_010888344.1; NZ_CP015081.1.
DR   PDB; 5KTE; X-ray; 3.94 A; A=26-436.
DR   PDB; 6BU5; X-ray; 2.40 A; A=35-436.
DR   PDB; 6C3I; X-ray; 2.95 A; A/B=1-436.
DR   PDB; 6D91; X-ray; 2.36 A; A=35-436.
DR   PDB; 6D9W; X-ray; 3.94 A; A=26-436.
DR   PDBsum; 5KTE; -.
DR   PDBsum; 6BU5; -.
DR   PDBsum; 6C3I; -.
DR   PDBsum; 6D91; -.
DR   PDBsum; 6D9W; -.
DR   AlphaFoldDB; Q9RTP8; -.
DR   SMR; Q9RTP8; -.
DR   STRING; 243230.DR_1709; -.
DR   TCDB; 2.A.55.3.7; the metal ion (mn(2+)-iron) transporter (nramp) family.
DR   ABCD; Q9RTP8; 1 sequenced antibody.
DR   EnsemblBacteria; AAF11265; AAF11265; DR_1709.
DR   KEGG; dra:DR_1709; -.
DR   PATRIC; fig|243230.17.peg.1920; -.
DR   eggNOG; COG1914; Bacteria.
DR   HOGENOM; CLU_020088_2_0_0; -.
DR   InParanoid; Q9RTP8; -.
DR   OMA; IATFVNS; -.
DR   OrthoDB; 416257at2; -.
DR   Proteomes; UP000002524; Chromosome I.
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:0015086; F:cadmium ion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005384; F:manganese ion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071281; P:cellular response to iron ion; IBA:GO_Central.
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   3D-structure; Cell membrane; Ion transport; Membrane; Reference proteome;
KW   Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..436
FT                   /note="Divalent metal cation transporter MntH"
FT                   /id="PRO_0000212616"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT   TRANSMEM        411..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           44..51
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           52..55
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           57..70
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   TURN            71..74
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           75..99
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           103..110
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           113..146
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           150..163
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           166..169
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           173..197
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           201..206
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           217..226
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           231..241
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   STRAND          248..250
FT                   /evidence="ECO:0007829|PDB:6BU5"
FT   HELIX           251..286
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   TURN            287..290
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   TURN            292..295
FT                   /evidence="ECO:0007829|PDB:6C3I"
FT   HELIX           297..307
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           310..342
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           349..366
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           370..395
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           399..402
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           403..405
FT                   /evidence="ECO:0007829|PDB:6D91"
FT   HELIX           409..434
FT                   /evidence="ECO:0007829|PDB:6D91"
SQ   SEQUENCE   436 AA;  46652 MW;  98776EF8B19103FA CRC64;
     MDSRSPSLPD DRPDPPEQHL DARAGATLRG TAGPRGVRRI LPFLGPAVIA SIAYMDPGNF
     ATNIEGGARY GYSLLWVILA ANLMAMVIQN LSANLGIASG RNLPELIRER WPRPLVWFYW
     IQAELVAMAT DLAEFLGAAL AIQLLTGLPM FWGAVVTGVV TFWLLNLQKR GTRPLELAVG
     AFVLMIGVAY LVQVVLARPD LAAVGAGFVP RLQGPGSAYL AVGIIGATVM PHVIYLHSAL
     TQGRIQTDTT EEKRRLVRLN RVDVIAAMGL AGLINMSMLA VAAATFHGKN VENAGDLTTA
     YQTLTPLLGP AASVLFAVAL LASGLSSSAV GTMAGDVIMQ GFMGFHIPLW LRRLITMLPA
     FIVILLGMDP SSVLILSQVI LCFGVPFALV PLLLFTARRD VMGALVTRRS FTVIGWVIAV
     IIIALNGYLL WELLGG
 
 
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