SBCC_STAA1
ID SBCC_STAA1 Reviewed; 1009 AA.
AC A7X203;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Nuclease SbcCD subunit C;
GN Name=sbcC; OrderedLocusNames=SAHV_1335;
OS Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=418127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu3 / ATCC 700698;
RX PubMed=17954695; DOI=10.1128/aac.00534-07;
RA Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT "Mutated response regulator graR is responsible for phenotypic conversion
RT of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT resistance to vancomycin-intermediate resistance.";
RL Antimicrob. Agents Chemother. 52:45-53(2008).
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; AP009324; BAF78218.1; -; Genomic_DNA.
DR RefSeq; WP_000803135.1; NC_009782.1.
DR AlphaFoldDB; A7X203; -.
DR KEGG; saw:SAHV_1335; -.
DR HOGENOM; CLU_004785_2_1_9; -.
DR OMA; ISHVQEM; -.
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; 2.
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_0000338466"
FT COILED 176..364
FT /evidence="ECO:0000255"
FT COILED 401..501
FT /evidence="ECO:0000255"
FT COILED 535..805
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; 117482 MW; 5CB8A758E8A5EA52 CRC64;
MKPLHLKLNN FGPFLKEEID FSKIDNNELF LISGKTGSGK TMIFDAMTYA LFGKASTEQR
EENDLRSHFA DGKQPMSVTF EFQLNHRIYK VHRQGPYIKE GNTTKTNAKF DVFEMVDGKY
EIRESKVISG TQFIIELLGV NADQFRQLFI LPQGEFKRFL ISNSREKQGI LRTLFDSEKF
EAIREILKEE LKKEKAQIEN RYQQIDLLWQ EIESFDDDKI KGLLELATQQ IDKLIENIPL
LQARSKEILA FVNESKETAI KEYEIIEKKT LENNILKDNI NQLNKNKIDF VQLKEQQPEI
DEIEAKLKLL QDITNLLNYI ENREKIETKI ANSKKDISKT NNKILNLDCD KRNIDKEKKM
LEENGDLIES KTSFIDKTRV LFNDINKYQQ SYLNIECLIT EGEQLGDELN NLIKGLEKVE
DSIGNNESDY EKIIELNNAI TNINNEINII KENEKAKAEL DKLLGSKQEL ENQINEETTI
MKNLEIKLDH YDKSKLDLND KESFISEIKS AVKIGDQCPI CGNEIQDLGH HIDFDSIAKR
QNEIKEIEAN IHAIKSNIAV HNSEIKFVNE KISNINIKTQ SDFSLEVLNK RLLENENALN
NQRDLNKFIE QMKEEKDNLT LQIHNKQLRL NKNESELKLC RDLITEFETL SKYNNITNFE
VDYKKYVQDV NQHQELSKEI EDKLMQLSQR KLIEQNNLNH YENQLETYNN DLELNEQSIE
MEMSRLNLTD DNDINEIIAW RGEQEELEQK RDTYKKRYHE FEMEIARLES LTKDKELLDS
DKLKDEYEQK KEKMNTLIDE YSAVHYQCQN NINKTQSIVS HINYLNQELK DQQEIFQLAE
IVSGKNNKNL TLENFVLIYY LDQIIAQANL RLATMSDNRY QLIRREAVSH GLSGLEIDVF
DLHSNKSRHI SSLSGGETFQ SSLALALGLS EIVQQQSGGI SLESIFIDEG FGTLDQETLE
TALDTLLNLK STGRMVGIIS HVSELKNRIP LVLEVKSDQY QSSTRFKRN