MNTH_STAAC
ID MNTH_STAAC Reviewed; 450 AA.
AC Q5HGX9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, 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=SACOL1114;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW37994.1; -; Genomic_DNA.
DR RefSeq; WP_001060842.1; NC_002951.2.
DR AlphaFoldDB; Q5HGX9; -.
DR SMR; Q5HGX9; -.
DR EnsemblBacteria; AAW37994; AAW37994; SACOL1114.
DR KEGG; sac:SACOL1114; -.
DR HOGENOM; CLU_020088_2_0_9; -.
DR OMA; SPKWLRY; -.
DR Proteomes; UP000000530; 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 membrane; Ion transport; Membrane; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..450
FT /note="Divalent metal cation transporter MntH"
FT /id="PRO_0000212634"
FT TRANSMEM 34..54
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 108..128
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 212..232
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00221"
SQ SEQUENCE 450 AA; 49724 MW; B5D111F877C8A63E CRC64;
MNNKRHSTNE QLSLDEINNT IKFDHRSSNK QKFLSFLGPG LLVAVGYMDP GNWITSMQGG
AQYGYTLLFV ILISSLSAML LQSMTVRLGI ATGMDLAQMT RHYLSRPIAI IFWIIAELAI
IATDIAEVIG SAIALNLLFN IPLIVGALIT VLDVFLLLFI MKYGFRKIEA IVGTLIFTVL
FIFIFEVYIS SPQLNAVLNG FIPHSEIITN NGILYIALGI IGATIMPHNL YLHSSIVQSR
TYSRHNNEEK AQAIKFATID SNIQLSIAFV VNCLLLVLGA SLFFNSNADD LGGFYDLYHA
LKTEPVLGAT MGAIMSTLFA VALLASGQNS TITGTLAGQI VMEGFLRLHI PNWLRRLITR
SLAVIPVIVC LIIFKGNAAK IEQLLVFSQV FLSIALPFCL IPLQLATSNK DLMGPFYNKT
WVNIISWTLI IILSILNVYL IVQTFQELQS