SBCC_BACSU
ID SBCC_BACSU Reviewed; 1130 AA.
AC O06714; O06712; O06713;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Nuclease SbcCD subunit C;
GN Name=sbcC; Synonyms=yirY; OrderedLocusNames=BSU10650;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353931; DOI=10.1099/00221287-143-10-3305;
RA Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.;
RT "Sequencing of regions downstream of addA (98 degrees) and citG (289
RT degrees) in Bacillus subtilis.";
RL Microbiology 143:3305-3308(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 227 AND 788-790.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
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=CAA70670.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA70671.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA70672.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Y09476; CAA70670.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Y09476; CAA70671.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Y09476; CAA70672.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB12905.2; -; Genomic_DNA.
DR PIR; A69836; A69836.
DR RefSeq; NP_388946.2; NC_000964.3.
DR RefSeq; WP_003245201.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O06714; -.
DR IntAct; O06714; 3.
DR STRING; 224308.BSU10650; -.
DR jPOST; O06714; -.
DR PaxDb; O06714; -.
DR PRIDE; O06714; -.
DR EnsemblBacteria; CAB12905; CAB12905; BSU_10650.
DR GeneID; 939784; -.
DR KEGG; bsu:BSU10650; -.
DR PATRIC; fig|224308.179.peg.1145; -.
DR eggNOG; COG0419; Bacteria.
DR InParanoid; O06714; -.
DR OMA; ISHVQEM; -.
DR PhylomeDB; O06714; -.
DR BioCyc; BSUB:BSU10650-MON; -.
DR Proteomes; UP000001570; 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; 2.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; DNA recombination; DNA replication; Endonuclease;
KW Exonuclease; Hydrolase; Nuclease; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1130
FT /note="Nuclease SbcCD subunit C"
FT /id="PRO_0000105861"
FT COILED 115..135
FT /evidence="ECO:0000255"
FT COILED 179..270
FT /evidence="ECO:0000255"
FT COILED 344..530
FT /evidence="ECO:0000255"
FT COILED 652..904
FT /evidence="ECO:0000255"
FT COILED 940..1004
FT /evidence="ECO:0000255"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 227
FT /note="A -> V (in Ref. 1; CAA70670)"
FT /evidence="ECO:0000305"
FT CONFLICT 788..790
FT /note="QIK -> PIQ (in Ref. 1; CAA70671)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1130 AA; 128921 MW; 3A53A1C0606210A9 CRC64;
MKPIALSIKG LHSFREEQTI DFEGLSGAGV FGIFGPTGSG KSSILDAMTL ALYGKVERAA
NNTHGILNHA EDTLSVSFTF ALQTNHQISY KVERVFKRTD EMKVKTALCR FIEIKDEHTV
LADKASEVNK RVEELLGLTI DDFTRAVVLP QGKFAEFLSL KGAERRHMLQ RLFNLEQYGD
RLVKKLRRQA QEANARKNEM LAEQSGLGEA SSEAVEQAEK VLEQAEARLE AMRKNRDQAK
ERFTEHQEIW NVQKEKSTYE EEEKRLAEEQ PHIDSMQKRL LEAETAAALK PYADRYAEAI
QHEEQAEKEQ TLAQKDLADR TAFFQQKHEE YEAWRQHKSE KEPELLAKQE QLSRLQEIEI
KLSEAKQEEE RKKADLRQKE EALQSVMNEL ETVTDRLTRG QNRQTELKQQ LKSLQVTSDE
RKSCQQAAEM ALRIRQTEEQ IKKEKKRSEE LNLVLQKMNE EKNTLVQKTE AEENNIIQAY
EAVQTVYHLV CETERSLTRM TEEARKSQHT LHLQREKARV ALLTKELAQK LTAGKPCPVC
GSTDHDPSAS VHETYEADSH LEEDIKRTDV LLTEAAALSQ EILSAKIMLE EQSARFIEQC
PFLQTIQAQN LEAAASFEHQ PVYEAFETAK FEWKRIKQDI LSVKTRMAQM IGAYQESLKK
AEQLNEKIGF EKREADRIES IISELQSSMD SSLNMFKEAF QNQSVDEAEK WQQAIEEKDR
AAEECEKRIE KSIAFLAEHE AQKEKLRESG HRLEREKLEL HYAAERIKSV IADYEHELGD
YAKGDSIQIK LRSVQQDLKL LKEKEQSLYE ELQSAQMKLN QAKSRASASE LTLQEAKGRL
EKAKAAWLEH TKNTSITRTE EVEQSLIPAD ELEKMKTGID QFMDKLKQNA ANLKRVAEIL
AGRALSESEW NETVAALQEA EDAFGAAIEE KGAAAKALAV IRDHHKRFNE IEAELKKWQM
HIDRLDKLQA VFKGNTFVEF LAEEQLESVA RDASARLSML TRQRYAIEVD SEGGFVMRDD
ANGGVRRPVS SLSGGETFLT SLSLALALSA QIQLRGEYPL QFFFLDEGFG TLDQDLLDTV
VTALEKLQSD NLAVGVISHV QELRARLPKK LIVHPAEPSG RGTRVSLELM
