SBCC_ECOLI
ID SBCC_ECOLI Reviewed; 1048 AA.
AC P13458; Q2MC29;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Nuclease SbcCD subunit C;
GN Name=sbcC; Synonyms=rmuA; OrderedLocusNames=b0397, JW0387;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2530497; DOI=10.1093/nar/17.20.8033;
RA Naom I.S., Morton S.J., Leach D.R.F., Lloyd R.G.;
RT "Molecular organization of sbcC, a gene that affects genetic recombination
RT and the viability of DNA palindromes in Escherichia coli K-12.";
RL Nucleic Acids Res. 17:8033-8046(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 378-1048.
RX PubMed=1744033; DOI=10.1128/jb.173.24.7765-7771.1991;
RA Reeder T.C., Schleif R.F.;
RT "Mapping, sequence, and apparent lack of function of araJ, a gene of the
RT Escherichia coli arabinose regulon.";
RL J. Bacteriol. 173:7765-7771(1991).
RN [6]
RP CHARACTERIZATION.
RX PubMed=1490631; DOI=10.1007/bf00120998;
RA Leach D.R.F., Lloyd R.G., Coulson A.F.;
RT "The SbcCD protein of Escherichia coli is related to two putative nucleases
RT in the UvrA superfamily of nucleotide-binding proteins.";
RL Genetica 87:95-100(1992).
RN [7]
RP CHARACTERIZATION.
RX PubMed=10886369; DOI=10.1046/j.1365-2443.2000.00341.x;
RA Slupska M.M., Chiang J.-H., Luther W.M., Stewart J.L., Amii L., Conrad A.,
RA Miller J.H.;
RT "Genes involved in the determination of the rate of inversions at short
RT inverted repeats.";
RL Genes Cells 5:425-437(2000).
RN [8]
RP CHARACTERIZATION.
RX PubMed=9653124; DOI=10.1073/pnas.95.14.7969;
RA Connelly J.C., Kirkham L.A., Leach D.R.;
RT "The SbcCD nuclease of Escherichia coli is a structural maintenance of
RT chromosomes (SMC) family protein that cleaves hairpin DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7969-7974(1998).
RN [9]
RP CHARACTERIZATION.
RX PubMed=9927737; DOI=10.1093/nar/27.4.1039;
RA Connelly J.C., de Leau E.S., Leach D.R.;
RT "DNA cleavage and degradation by the SbcCD protein complex from Escherichia
RT coli.";
RL Nucleic Acids Res. 27:1039-1046(1999).
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.
CC -!- SUBUNIT: Heterodimer of SbcC and SbcD.
CC -!- INTERACTION:
CC P13458; P76092: ynbC; NbExp=3; IntAct=EBI-546919, EBI-544837;
CC -!- SIMILARITY: Belongs to the SMC family. SbcC subfamily. {ECO:0000305}.
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DR EMBL; X15981; CAA34104.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18121.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73500.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76177.1; -; Genomic_DNA.
DR EMBL; M64787; AAA23473.1; -; Genomic_DNA.
DR PIR; JS0350; BVECSC.
DR RefSeq; NP_414931.1; NC_000913.3.
DR RefSeq; WP_000698951.1; NZ_SSZK01000009.1.
DR PDB; 6S6V; EM; 3.50 A; C/D=1-1048.
DR PDB; 6S85; EM; 4.20 A; C/D=1-1048.
DR PDBsum; 6S6V; -.
DR PDBsum; 6S85; -.
DR AlphaFoldDB; P13458; -.
DR SMR; P13458; -.
DR BioGRID; 4259821; 33.
DR BioGRID; 853317; 1.
DR ComplexPortal; CPX-4021; sbcCD DNA exo/endonuclease complex.
DR DIP; DIP-342N; -.
DR IntAct; P13458; 6.
DR STRING; 511145.b0397; -.
DR jPOST; P13458; -.
DR PaxDb; P13458; -.
DR PRIDE; P13458; -.
DR EnsemblBacteria; AAC73500; AAC73500; b0397.
DR EnsemblBacteria; BAE76177; BAE76177; BAE76177.
DR GeneID; 949076; -.
DR KEGG; ecj:JW0387; -.
DR KEGG; eco:b0397; -.
DR PATRIC; fig|1411691.4.peg.1882; -.
DR EchoBASE; EB0920; -.
DR eggNOG; COG0419; Bacteria.
DR HOGENOM; CLU_004785_1_0_6; -.
DR InParanoid; P13458; -.
DR OMA; ISHVQEM; -.
DR PhylomeDB; P13458; -.
DR BioCyc; EcoCyc:EG10927-MON; -.
DR BioCyc; MetaCyc:EG10927-MON; -.
DR PRO; PR:P13458; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990391; C:DNA repair complex; IPI:ComplexPortal.
DR GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IDA:EcoCyc.
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:1990238; F:double-stranded DNA endodeoxyribonuclease activity; IDA:EcoCyc.
DR GO; GO:0004529; F:exodeoxyribonuclease activity; IDA:EcoCyc.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:EcoCyc.
DR GO; GO:0006310; P:DNA recombination; IC:ComplexPortal.
DR GO; GO:0006281; P:DNA repair; IDA:EcoCyc.
DR GO; GO:0006260; P:DNA replication; IDA:EcoCyc.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR004592; SbcC_gammaproteobac_type.
DR Pfam; PF13476; AAA_23; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00618; sbcc; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coiled coil; DNA recombination; DNA replication;
KW Endonuclease; Exonuclease; Hydrolase; Nuclease; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1048
FT /note="Nuclease SbcCD subunit C"
FT /id="PRO_0000105864"
FT COILED 191..402
FT /evidence="ECO:0000255"
FT COILED 438..502
FT /evidence="ECO:0000255"
FT COILED 528..648
FT /evidence="ECO:0000255"
FT COILED 671..695
FT /evidence="ECO:0000255"
FT COILED 770..880
FT /evidence="ECO:0000255"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 2..14
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 25..30
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 77..87
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6S6V"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 880..886
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 890..892
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 894..918
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 920..926
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 928..931
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 934..938
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 941..943
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 948..950
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 953..969
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 980..982
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 991..999
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 1000..1006
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 1011..1014
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 1020..1023
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 1025..1029
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 1043..1045
FT /evidence="ECO:0007829|PDB:6S6V"
SQ SEQUENCE 1048 AA; 118721 MW; BF873BC3386F98C4 CRC64;
MKILSLRLKN LNSLKGEWKI DFTREPFASN GLFAITGPTG AGKTTLLDAI CLALYHETPR
LSNVSQSQND LMTRDTAECL AEVEFEVKGE AYRAFWSQNR ARNQPDGNLQ VPRVELARCA
DGKILADKVK DKLELTATLT GLDYGRFTRS MLLSQGQFAA FLNAKPKERA ELLEELTGTE
IYGQISAMVF EQHKSARTEL EKLQAQASGV TLLTPEQVQS LTASLQVLTD EEKQLITAQQ
QEQQSLNWLT RQDELQQEAS RRQQALQQAL AEEEKAQPQL AALSLAQPAR NLRPHWERIA
EHSAALAHIR QQIEEVNTRL QSTMALRASI RHHAAKQSAE LQQQQQSLNT WLQEHDRFRQ
WNNEPAGWRA QFSQQTSDRE HLRQWQQQLT HAEQKLNALA AITLTLTADE VATALAQHAE
QRPLRQHLVA LHGQIVPQQK RLAQLQVAIQ NVTQEQTQRN AALNEMRQRY KEKTQQLADV
KTICEQEARI KTLEAQRAQL QAGQPCPLCG STSHPAVEAY QALEPGVNQS RLLALENEVK
KLGEEGATLR GQLDAITKQL QRDENEAQSL RQDEQALTQQ WQAVTASLNI TLQPLDDIQP
WLDAQDEHER QLRLLSQRHE LQGQIAAHNQ QIIQYQQQIE QRQQLLLTTL TGYALTLPQE
DEEESWLATR QQEAQSWQQR QNELTALQNR IQQLTPILET LPQSDELPHC EETVVLENWR
QVHEQCLALH SQQQTLQQQD VLAAQSLQKA QAQFDTALQA SVFDDQQAFL AALMDEQTLT
QLEQLKQNLE NQRRQAQTLV TQTAETLAQH QQHRPDDGLA LTVTVEQIQQ ELAQTHQKLR
ENTTSQGEIR QQLKQDADNR QQQQTLMQQI AQMTQQVEDW GYLNSLIGSK EGDKFRKFAQ
GLTLDNLVHL ANQQLTRLHG RYLLQRKASE ALEVEVVDTW QADAVRDTRT LSGGESFLVS
LALALALSDL VSHKTRIDSL FLDEGFGTLD SETLDTALDA LDALNASGKT IGVISHVEAM
KERIPVQIKV KKINGLGYSK LESTFAVK
