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SCDA_STAAR
ID   SCDA_STAAR              Reviewed;         224 AA.
AC   Q6GK53;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Iron-sulfur cluster repair protein ScdA {ECO:0000255|HAMAP-Rule:MF_01156};
GN   Name=scdA {ECO:0000255|HAMAP-Rule:MF_01156}; OrderedLocusNames=SAR0256;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Di-iron-containing protein involved in the repair of iron-
CC       sulfur clusters damaged by oxidative and nitrosative stress conditions.
CC       {ECO:0000255|HAMAP-Rule:MF_01156}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01156}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01156}.
CC   -!- SIMILARITY: Belongs to the RIC family. ScdA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01156}.
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DR   EMBL; BX571856; CAG39282.1; -; Genomic_DNA.
DR   RefSeq; WP_000608835.1; NC_002952.2.
DR   AlphaFoldDB; Q6GK53; -.
DR   SMR; Q6GK53; -.
DR   KEGG; sar:SAR0256; -.
DR   HOGENOM; CLU_076075_0_1_9; -.
DR   OMA; ACTTWRV; -.
DR   OrthoDB; 1701106at2; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0051409; P:response to nitrosative stress; IEA:UniProtKB-UniRule.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.3910.10; -; 1.
DR   HAMAP; MF_01156; RIC_ScdA; 1.
DR   InterPro; IPR012312; Hemerythrin-like.
DR   InterPro; IPR019903; RIC_family.
DR   InterPro; IPR023551; ScdA.
DR   InterPro; IPR038062; ScdA-like_N_sf.
DR   PANTHER; PTHR36438; PTHR36438; 1.
DR   Pfam; PF01814; Hemerythrin; 1.
DR   Pfam; PF04405; ScdA_N; 1.
DR   SUPFAM; SSF140683; SSF140683; 1.
DR   TIGRFAMs; TIGR03652; FeS_repair_RIC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Iron; Metal-binding; Stress response.
FT   CHAIN           1..224
FT                   /note="Iron-sulfur cluster repair protein ScdA"
FT                   /id="PRO_0000220338"
SQ   SEQUENCE   224 AA;  25514 MW;  A5ACF79CE590880C CRC64;
     MINKNDIVAD VVTDYPKAAD IFRSVGIDFC CGGQVSIEAA SLEKKNVDLN ELLQRLNEVE
     QTNTPGSLNP KFLNVSSLIQ YIQSAYHEPL REEFKNLTPY VTKLSKVHGP NHPYLVELKE
     TYDTFKNGML EHMQKEDDVD FPKLIKYEQG EVVDDINTVI DDLVSDHIAT GQLLVKMSEL
     TSSYEPPIEA CGTWRLVYQR LKALEVLTHE HVHLENHVLF KKVS
 
 
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