SBCC_LACLA
ID SBCC_LACLA Reviewed; 1046 AA.
AC Q9CFZ0;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Nuclease SbcCD subunit C;
GN Name=sbcC; OrderedLocusNames=LL1321; ORFNames=L152588;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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; AE005176; AAK05419.1; -; Genomic_DNA.
DR PIR; A86790; A86790.
DR RefSeq; NP_267477.1; NC_002662.1.
DR RefSeq; WP_010905885.1; NC_002662.1.
DR AlphaFoldDB; Q9CFZ0; -.
DR STRING; 272623.L152588; -.
DR PaxDb; Q9CFZ0; -.
DR PRIDE; Q9CFZ0; -.
DR EnsemblBacteria; AAK05419; AAK05419; L152588.
DR KEGG; lla:L152588; -.
DR PATRIC; fig|272623.7.peg.1425; -.
DR eggNOG; COG0419; Bacteria.
DR HOGENOM; CLU_004785_2_0_9; -.
DR OMA; ISHVQEM; -.
DR Proteomes; UP000002196; 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; Reference proteome.
FT CHAIN 1..1046
FT /note="Nuclease SbcCD subunit C"
FT /id="PRO_0000105865"
FT COILED 223..239
FT /evidence="ECO:0000255"
FT COILED 268..432
FT /evidence="ECO:0000255"
FT COILED 468..505
FT /evidence="ECO:0000255"
FT COILED 543..867
FT /evidence="ECO:0000255"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1046 AA; 120200 MW; 8F70D00AC28F8691 CRC64;
MKPIYLEMNY FGPHENSVVD FRLLDESPIF LISGDTGAGK STIFDAMTYA LFGTTTGDRD
AKEMRSQFAT ADDRTSVTFY FKQGNLLYRI ERSPEQKLSK KRGSGSTLQK STAKLAIVDR
VKGIEKNNIA INPKNVGEEI TRLLHLNAEQ FKKIILLPQN DFSRFLKSST PDKEAILKRI
FGTYIFTSFS NEIKAKNSEM NAVYLEYDRK QQNLYESSIW NPIELKELED AAEQEKLDLV
TSLWKDRVAR KNEIEGQTFE QEEKVISIEI AYKSALELEN QFKNLNNLEN DYQQNIIEKS
AIFEENSEYL KKLKWAFPLK ESIHELEQDI KQSKSVKNNI AGIISEKAKD EILLKKLTNE
KEDLNKQQEN INENKKVAEK IFIQIQLSLQ VEKKQSKVEE LKLEQADNLT LLESFKANLG
QAAENISTLQ DDVISDDYFI NKREERNQLE LTFRGKLIPT FQKVKHSKDD IVGLELKLKE
NTIALSENKD NLEKAKFAYN EKLKGRRRLM IAQLQSELQE GEACPVCGAL EHPFTETIEE
SSYKELGNLL KEIDESQKKQ TVLLEKNKQL QQLKTELKTS LDLKKIEADE FEKELSILYS
EFIADYSQIF PDSFDEVSID ESLLNLTKSL ELEEVKNDET KVKLADLESK KLELQEKVKD
FEYSNQEFNR QIENLNAEIT EIGITETSYN LIRKRNRLME KADLFEKHLS ELMAQLSDIK
IKISSQTASL NSFESQEATL LERISANKEK IKEKFSEQEA FTTEFQILKE WAYDDDLIQI
SQKVEQYKAD KARLKVEIKN IQQLIQNKKR PNLALIEEEK KQTNENYVFL QKKLVSAENE
VEQAKSILSE LKKVIKQQDK DASKKSAITK LYNAISGRAS EDKLRLETYV VQNYLEKILD
YANLHFINQL SNNRYRFELA GEGNNRRMDH GLDINIYDNE TGAARSADTL SGGETFIAAL
SIALALSEVV QNTANGVQIE ALFIDEGFGS LDQETLQKAM QALEQIGENR LVGVISHVEE
MKATIGQRII INKMGDGRSN IKSVIK