ID   MNTC_BACSU              Reviewed;         435 AA.
AC   O35024;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Manganese transport system membrane protein MntC;
GN   Name=mntC {ECO:0000303|PubMed:10760146}; Synonyms=ytgC;
GN   OrderedLocusNames=BSU30750;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   POSSIBLE FUNCTION.
RX   PubMed=10760146; DOI=10.1046/j.1365-2958.2000.01811.x;
RA   Que Q., Helmann J.D.;
RT   "Manganese homeostasis in Bacillus subtilis is regulated by MntR, a
RT   bifunctional regulator related to the diphtheria toxin repressor family of
RT   proteins.";
RL   Mol. Microbiol. 35:1454-1468(2000).
RN   [4]
RP   INDUCTION.
RX   PubMed=12950915; DOI=10.1046/j.1365-2958.2003.03648.x;
RA   Guedon E., Moore C.M., Que Q., Wang T., Ye R.W., Helmann J.D.;
RT   "The global transcriptional response of Bacillus subtilis to manganese
RT   involves the MntR, Fur, TnrA and sigmaB regulons.";
RL   Mol. Microbiol. 49:1477-1491(2003).
CC   -!- FUNCTION: Probably part of the ABC transporter complex MntABCD involved
CC       in manganese import. Probably responsible for the translocation of the
CC       substrate across the membrane. {ECO:0000305|PubMed:10760146}.
CC   -!- SUBUNIT: The complex is probably composed of two ATP-binding proteins
CC       (MntB), two transmembrane proteins (MntC and MntD) and a solute-binding
CC       protein (MntA). {ECO:0000305|PubMed:10760146}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Repressed by MntR in the presence of manganese.
CC       {ECO:0000269|PubMed:12950915}.
CC   -!- SIMILARITY: Belongs to the ABC-3 integral membrane protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF008220; AAC00231.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15053.1; -; Genomic_DNA.
DR   PIR; D69992; D69992.
DR   RefSeq; NP_390953.1; NC_000964.3.
DR   RefSeq; WP_003229064.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O35024; -.
DR   SMR; O35024; -.
DR   STRING; 224308.BSU30750; -.
DR   PaxDb; O35024; -.
DR   PRIDE; O35024; -.
DR   EnsemblBacteria; CAB15053; CAB15053; BSU_30750.
DR   GeneID; 937203; -.
DR   KEGG; bsu:BSU30750; -.
DR   PATRIC; fig|224308.179.peg.3333; -.
DR   eggNOG; COG1108; Bacteria.
DR   eggNOG; COG1321; Bacteria.
DR   InParanoid; O35024; -.
DR   OMA; LCIFWRA; -.
DR   PhylomeDB; O35024; -.
DR   BioCyc; BSUB:BSU30750-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0010043; P:response to zinc ion; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.3470.10; -; 1.
DR   InterPro; IPR037294; ABC_BtuC-like.
DR   InterPro; IPR001626; ABC_TroCD.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR30477; PTHR30477; 1.
DR   Pfam; PF00950; ABC-3; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF81345; SSF81345; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Ion transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..435
FT                   /note="Manganese transport system membrane protein MntC"
FT                   /id="PRO_0000171150"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   435 AA;  47945 MW;  68E6D590D90A73BC CRC64;
     MFESLWLQLQ HPNTQWVLAG TLLLGTASGV LGSFVLLRKQ SLIGDAMAHS ALPGVCLAFL
     FTGQKSLPFF LLGAALAGLL GTFCIQLIPR LSKTKEDSAI GIVLSVFFGV GIILLTYIQQ
     QGAGSQSGLD SFLFGQAASL VRQDIILIAG ISAVLLLLCI VFFKEFTLIT FDLAFAKGLG
     IPVRFLNGLL ACLIVCAVVI GLQTVGVILM AAMLITPAIT ARYWTERLTG MIIIAGITGG
     VSGVAGTLLS TTMKGMATGP LMILSATLLF LFSMICAPKR GLAAKAIRLM RLRRRTSREQ
     VLLAIYEQYE KNNLCVTVES VRKKRRLSPS LCLKALNDLE QERCIERIEN GIWQITSKGI
     EKGYHTALKQ RMYEVYLMHE MELANIESDQ DYFDPDRLPR ETRERLYSLL KLYGRMPERR
     KASHDAEKGQ IANEF