SBCC_STAA3
ID SBCC_STAA3 Reviewed; 1009 AA.
AC Q2FH88;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Nuclease SbcCD subunit C;
GN Name=sbcC; OrderedLocusNames=SAUSA300_1243;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
CC -!- FUNCTION: SbcCD cleaves DNA hairpin structures. These structures can
CC inhibit DNA replication and are intermediates in certain DNA
CC recombination reactions. The complex acts as a 3'->5' double strand
CC exonuclease that can open hairpins. It also has a 5' single-strand
CC endonuclease activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of SbcC and SbcD. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SbcC subfamily. {ECO:0000305}.
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DR EMBL; CP000255; ABD20847.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2FH88; -.
DR SMR; Q2FH88; -.
DR PRIDE; Q2FH88; -.
DR EnsemblBacteria; ABD20847; ABD20847; SAUSA300_1243.
DR KEGG; saa:SAUSA300_1243; -.
DR HOGENOM; CLU_004785_2_1_9; -.
DR Proteomes; UP000001939; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR Pfam; PF13476; AAA_23; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; DNA recombination; DNA replication; Endonuclease;
KW Exonuclease; Hydrolase; Nuclease; Nucleotide-binding.
FT CHAIN 1..1009
FT /note="Nuclease SbcCD subunit C"
FT /id="PRO_0000338473"
FT COILED 176..364
FT /evidence="ECO:0000255"
FT COILED 392..502
FT /evidence="ECO:0000255"
FT COILED 535..802
FT /evidence="ECO:0000255"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1009 AA; 117283 MW; 8F4513CE540CE036 CRC64;
MKPLHLKLNN FGPFLKEEID FSKIDNNELF LISGKTGSGK TMIFDAMTYA LFGKASTEQR
EENDLRSHFA DGKQPMSVTF EFQLNHRIYK VHRQGPYIKE GNTTKTNAKF DVFEMVDGKY
EIRESKVISG TQFIIELLGV NADQFRQLFI LPQGEFKRFL ISNSREKQGI LRTLFDSEKF
EAIREILKEE VKKEKAQIEN RYQQIDLLWQ EIESFDDDNI KGLLEVATQQ IDKLIENIPL
LQARSKEILA SVNESKETAI KEFEIIEKKT LENNILKDNI NQLNKNKIDF VQLKEQQPEI
EGIEAKLKLL QDITNLLNYI ENREKIETKI ANSKKDISKT NNKILNLDCD KRNIDKEKKM
LEENGDLIES KISFIDKTRV LFNDINKYQQ SYLNIERLRT EGEQLGDELN DLIKGLETVE
DSIGNNQSDY EKIIELNNTI TNINNEINII KENEKAKAEL DKLLGSKQEL ENQINEETSI
LKNLEIKLDR YDKTKLDLND KESFISEIKS AVNIGDQCPI CGNEIQDLGH HIDFDSIAKR
QNEIKEIEAN IHAIKSNIAV HNSEIKFVNE KISNINIKTQ SDFSLEVLNK RLLENENALN
NQRDLNKFIE QMKEEKDNLT LQIHNKQLRL NKNESELKLC RDLITEFETL SKYNNITNFE
VDYKKYVQDV NQHQELSKEI EDKLMQLSQR KLIEQNNLNH YENQLETYNN DLELNEQSIE
MEMSRLNLTD DNDIDEIIAW RGEQEELEQK RDTYKKRYHE IEMEIARLES LTKDKELLDS
DKLKDEYELK KGKMNTLIDE YSAVHYQCQN NINKTQSIVS HINYLNQELK DQQEIFQLAE
IVSGKNNKNL TLENFVLIYY LDQIIAQANL RLATMSDNRY QLIRREAVSH GLSGLEIDVF
DLHSNKSRHI SSLSGGETFQ SSLALALGLS EIVQQQSGGI SLESIFIDEG FGTLDQETLE
TALDTLLNLK STGRMVGIIS HVSELKNRIP LVLEVKSDQY QSSTRFKRN