APBC_BACSU
ID APBC_BACSU Reviewed; 352 AA.
AC P50863;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040};
GN Name=salA; Synonyms=mrp, rec233, ybaL, ybxI; OrderedLocusNames=BSU01540;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7559346; DOI=10.1128/jb.177.19.5582-5589.1995;
RA Sekiguchi J., Akeo K., Yamamoto H., Khasanov F.K., Alonso J.C., Kuroda A.;
RT "Nucleotide sequence and regulation of a new putative cell wall hydrolase
RT gene, cwlD, which affects germination in Bacillus subtilis.";
RL J. Bacteriol. 177:5582-5589(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969501; DOI=10.1099/13500872-142-11-3039;
RA Yasumoto K., Liu H., Jeong S.M., Ohashi Y., Kakinuma S., Tanaka K.,
RA Kawamura F., Yoshikawa H., Takahashi H.;
RT "Sequence analysis of a 50 kb region between spo0H and rrnH on the Bacillus
RT subtilis chromosome.";
RL Microbiology 142:3039-3046(1996).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 328-352.
RC STRAIN=168;
RX PubMed=2517635; DOI=10.1099/00221287-135-12-3431;
RA Yon J.R., Sammons R.L., Smith D.A.;
RT "Cloning and sequencing of the gerD gene of Bacillus subtilis.";
RL J. Gen. Microbiol. 135:3431-3445(1989).
RN [5]
RP FUNCTION.
RX PubMed=15126467; DOI=10.1128/jb.186.10.3056-3064.2004;
RA Ogura M., Matsuzawa A., Yoshikawa H., Tanaka T.;
RT "Bacillus subtilis SalA (YbaL) negatively regulates expression of scoC,
RT which encodes the repressor for the alkaline exoprotease gene, aprE.";
RL J. Bacteriol. 186:3056-3064(2004).
RN [6]
RP INTERACTION WITH BRXC, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=168 / CU1065 {ECO:0000303|PubMed:33722570};
RX PubMed=33722570; DOI=10.1016/j.redox.2021.101935;
RA Gaballa A., Su T.T., Helmann J.D.;
RT "The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr
RT (YpdA) disulfide reductase reduce S-bacillithiolated proteins.";
RL Redox Biol. 42:101935-101935(2021).
CC -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to target
CC apoproteins. Can hydrolyze ATP. {ECO:0000255|HAMAP-Rule:MF_02040}.
CC -!- FUNCTION: Negatively regulates the expression of hpr/scoC. The effect
CC on hpr/scoC may be indirect. {ECO:0000269|PubMed:15126467}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with BrxC
CC (PubMed:33722570). {ECO:0000255|HAMAP-Rule:MF_02040,
CC ECO:0000269|PubMed:33722570}.
CC -!- INDUCTION: Autoregulated.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC {ECO:0000255|HAMAP-Rule:MF_02040}.
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DR EMBL; X74737; CAA52756.1; -; Genomic_DNA.
DR EMBL; D64126; BAA10994.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11930.1; -; Genomic_DNA.
DR EMBL; M27259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A69743; A69743.
DR RefSeq; NP_388035.1; NC_000964.3.
DR RefSeq; WP_003235124.1; NZ_JNCM01000029.1.
DR AlphaFoldDB; P50863; -.
DR SMR; P50863; -.
DR IntAct; P50863; 5.
DR MINT; P50863; -.
DR STRING; 224308.BSU01540; -.
DR jPOST; P50863; -.
DR PaxDb; P50863; -.
DR PRIDE; P50863; -.
DR EnsemblBacteria; CAB11930; CAB11930; BSU_01540.
DR GeneID; 938914; -.
DR KEGG; bsu:BSU01540; -.
DR PATRIC; fig|224308.179.peg.158; -.
DR eggNOG; COG0489; Bacteria.
DR InParanoid; P50863; -.
DR OMA; PDNHPSE; -.
DR PhylomeDB; P50863; -.
DR BioCyc; BSUB:BSU01540-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:CACAO.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR000808; Mrp_CS.
DR InterPro; IPR044304; NUBPL-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR42961; PTHR42961; 1.
DR Pfam; PF10609; ParA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01215; MRP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..352
FT /note="Iron-sulfur cluster carrier protein"
FT /id="PRO_0000184929"
FT BINDING 114..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02040"
FT CONFLICT 328
FT /note="D -> Y (in Ref. 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 38639 MW; 255633623E8623DB CRC64;
MIREDEVRKL VGEMREPFLQ RPLGELDAVK EIKIKPEKRH ISVKVALAKT GTAEQMQIQQ
EIVNVLKGAG AETVGLRFEE LPEETVAKFR APSAEKKTLL NMDNPPVFLA VASGKGGVGK
STVSVNLAIS LARLGKKVGL IDADIYGFSV PDMMGITVRP TIEGEKLLPV ERFGVKVMSM
GFFVEENAPV VWRGPMLGKM LNNFFHEVEW GEVDYIVLDL PPGTGDVALD VHTMLPSCKE
IIVSTPHPTA AFVAARAGSM AIKTDHEVVG VIENMAYYES AKTGEREYVF GKGGGDKLAE
ELNVPLLGRI PLKQPDWDKD QFAPSVYDEN HPIGEIYQDI AKKIDAKMSV QV
