MNTA_BACSU
ID MNTA_BACSU Reviewed; 306 AA.
AC O34385;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Manganese-binding lipoprotein MntA;
DE Flags: Precursor;
GN Name=mntA {ECO:0000303|PubMed:10760146}; Synonyms=ytgA;
GN OrderedLocusNames=BSU30770;
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, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
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).
RN [5]
RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
CC -!- FUNCTION: Probably part of the ABC transporter complex MntABCD involved
CC in manganese import.
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) (Probable). Interacts with FloT (PubMed:23651456).
CC {ECO:0000269|PubMed:23651456, ECO:0000305|PubMed:10760146}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23651456,
CC ECO:0000305}; Lipid-anchor {ECO:0000305}. Membrane raft
CC {ECO:0000269|PubMed:23651456}; Lipid-anchor. Note=Present in detergent-
CC resistant membrane (DRM) fractions that may be equivalent to eukaryotic
CC membrane rafts; these rafts include proteins involved in signaling,
CC molecule trafficking and protein secretion.
CC {ECO:0000269|PubMed:23651456}.
CC -!- INDUCTION: Repressed by MntR in the presence of manganese.
CC {ECO:0000269|PubMed:12950915}.
CC -!- DISRUPTION PHENOTYPE: Null mutant is very sensitive to manganese.
CC {ECO:0000269|PubMed:10760146}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC {ECO:0000305}.
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DR EMBL; AF008220; AAC00229.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15055.1; -; Genomic_DNA.
DR PIR; B69992; B69992.
DR RefSeq; NP_390955.1; NC_000964.3.
DR RefSeq; WP_003229060.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34385; -.
DR SMR; O34385; -.
DR STRING; 224308.BSU30770; -.
DR jPOST; O34385; -.
DR PaxDb; O34385; -.
DR PRIDE; O34385; -.
DR EnsemblBacteria; CAB15055; CAB15055; BSU_30770.
DR GeneID; 937219; -.
DR KEGG; bsu:BSU30770; -.
DR PATRIC; fig|224308.179.peg.3335; -.
DR eggNOG; COG0803; Bacteria.
DR InParanoid; O34385; -.
DR OMA; DPHIWFD; -.
DR PhylomeDB; O34385; -.
DR BioCyc; BSUB:BSU30770-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0030001; P:metal ion transport; IEA:InterPro.
DR InterPro; IPR006129; AdhesinB.
DR InterPro; IPR006128; Lipoprotein_4.
DR InterPro; IPR006127; ZnuA-like.
DR Pfam; PF01297; ZnuA; 1.
DR PRINTS; PR00691; ADHESINB.
DR PRINTS; PR00690; ADHESNFAMILY.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Metal-binding; Palmitate;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT CHAIN 19..306
FT /note="Manganese-binding lipoprotein MntA"
FT /id="PRO_0000031880"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 33418 MW; FD6AFD3B07148127 CRC64;
MRQGLMAAVL FATFALTGCG TDSAGKSADQ QLQVTATTSQ IADAAENIGG KHVKVTSLMG
PGVDPHLYKA SQGDTKKLMS ADVVLYSGLH LEGKMEDVLQ KIGEQKQSAA VAEAIPKNKL
IPAGEGKTFD PHVWFSIPLW IYAVDEIEAQ FSKAMPQHAD AFRKNAKEYK EDLQYLDKWS
RKEIAHIPEK SRVLVTAHDA FAYFGNEYGF KVKGLQGLST DSDYGLRDVQ ELVDLLTEKQ
IKAVFVESSV SEKSINAVVE GAKEKGHTVT IGGQLYSDAM GEKGTKEGTY EGMFRHNINT
ITKALK
