SBCC_STAAB
ID SBCC_STAAB Reviewed; 1009 AA.
AC Q2YXX0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Nuclease SbcCD subunit C;
GN Name=sbcC; OrderedLocusNames=SAB1204;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI80893.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ938182; CAI80893.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q2YXX0; -.
DR KEGG; sab:SAB1204; -.
DR HOGENOM; CLU_004785_2_1_9; -.
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_0000338460"
FT COILED 176..208
FT /evidence="ECO:0000255"
FT COILED 264..364
FT /evidence="ECO:0000255"
FT COILED 392..501
FT /evidence="ECO:0000255"
FT COILED 535..776
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; 117613 MW; C18A8803F74B0F8F CRC64;
MKPLHLKLNN FGPFLKEEID FSKIDNNELF LISGKTGSGK TMIFDAMTYA LFGKASTEQR
EENDLRSHFA DGKQPMSVTF EFQLNHRIYK VHRQGPYIKE GNTTKTNAKF DVFEMVDGKY
EIRESKVISG TQFIIELLGV NADQFRQLFI LPQGEFKRFL ISNSREKQGI LRTLFDSEKF
EAIREILKEE VKKEKAQIEN RYQQIDLLWQ EIESFDDDKI KGLLEVATQQ IDKVIENIPL
LQVRSKEILA FVNESKETAI KEYEIIEKKT LENNILKDNI NQLNKNKIDF VQLKEQQPEI
EEIEAKLKLL QDITNLLNYI ENREKIETKI ANCKKDISKT NNKILNLECD KRTIDKEKKM
LEENGDLIES KISFIDKTRV LFNDINKYQQ SYLNIERLRT EGEQLGDELN NLIKGLEKVE
DSIGNNESDY EKIIELNNAI TNINNEINVI KENEKAKAEL DKLLGSKQEL ENQINEEKTI
LKNLEIKLDR YDKSKLDLND KESFISEIKS AVKIGDQCPI CGNEIQDLGH HIDFDSIAKR
QNEIKEIEAN IHTMKSNIAV HNFEIKFVNE KISNINIKTQ SDLSLEVLNK RLLENENALN
NQRDLNKFIE QMKEEKDNLT LQIHNKQLRL NKNESELKIC RDLITEFETL SKYNNITNFE
VDYKKYVQDV NQHQEHSKEI EDKLIQLSQR KLIEQNNLNH YENQLETYNN DLELNEQSIE
MEMSRLNLTD DNDINEIIAW RGEQEELEQK RDTYKKRYHE FEMEIARLES LTKDKELLDS
DKLIDEYELK KGKMNTLIDE YSAVHYQCQN NIKKTQSIVS HINYLNQELK DQQEIFQLAE
IVSGKNNKNL TLENFVLIYY LDQIIAQANL RLATMSDNRY QLIRREAVSH GLSGLEIDVF
DLHSNKSRHI SSLSGGETFQ SSLALALGLS EIVQQQSGGI SLESIFIDEG FGTLDQETLE
TALDTLLNLK STGRMVGIIS HVSELKNRIP LVLEVKSDQY QSSTRFKRN