ID   SCDA_STAAS              Reviewed;         224 AA.
AC   Q6GCL3;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=SAS0236;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
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; BX571857; CAG42006.1; -; Genomic_DNA.
DR   RefSeq; WP_000608831.1; NC_002953.3.
DR   AlphaFoldDB; Q6GCL3; -.
DR   SMR; Q6GCL3; -.
DR   KEGG; sas:SAS0236; -.
DR   HOGENOM; CLU_076075_0_1_9; -.
DR   OMA; ACTTWRV; -.
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_0000220339"
SQ   SEQUENCE   224 AA;  25470 MW;  C6F4DC880C1B6A7C CRC64;
     MINKNDIVAD VVTDYPKAAD IFRSVGIDFC CGGQVSIEAA SLEKKNVDLN ELLQRLNDVE
     QTNTPGSLNP KFLNVSSLIQ YIQAAYHEPL REEFKNLTPY VTKLSKVHGP NHPYLVELKE
     TYDTFKNGML EHMQKEDDVD FPKLIKYEQG EVVDDINTVI DDLVSDHIAT GQLLVKMSDL
     TSSYEPPIEA CGTWRLVYQR LKALEVLTHE HVHLENHVLF KKVS