SBCD_ECOLI
ID SBCD_ECOLI Reviewed; 400 AA.
AC P0AG76; P13457; Q2MC28;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Nuclease SbcCD subunit D;
GN Name=sbcD; Synonyms=yajA; OrderedLocusNames=b0398, JW0388;
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 CHARACTERIZATION.
RX PubMed=1531222; DOI=10.1128/jb.174.4.1222-1228.1992;
RA Gibson F.P., Leach D.R.F., Lloyd R.G.;
RT "Identification of sbcD mutations as cosuppressors of recBC that allow
RT propagation of DNA palindromes in Escherichia coli K-12.";
RL J. Bacteriol. 174:1222-1228(1992).
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=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 [8]
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 -!- SIMILARITY: Belongs to the SbcD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18122.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X15981; CAA34103.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18122.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73501.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76178.1; -; Genomic_DNA.
DR PIR; JS0349; JS0349.
DR RefSeq; NP_414932.1; NC_000913.3.
DR RefSeq; WP_001221319.1; NZ_STEB01000007.1.
DR PDB; 6S6V; EM; 3.50 A; A/B=1-400.
DR PDB; 6S85; EM; 4.20 A; A/B=1-400.
DR PDBsum; 6S6V; -.
DR PDBsum; 6S85; -.
DR AlphaFoldDB; P0AG76; -.
DR SMR; P0AG76; -.
DR BioGRID; 4262090; 138.
DR BioGRID; 849438; 2.
DR ComplexPortal; CPX-4021; sbcCD DNA exo/endonuclease complex.
DR DIP; DIP-10828N; -.
DR IntAct; P0AG76; 5.
DR STRING; 511145.b0398; -.
DR jPOST; P0AG76; -.
DR PaxDb; P0AG76; -.
DR PRIDE; P0AG76; -.
DR EnsemblBacteria; AAC73501; AAC73501; b0398.
DR EnsemblBacteria; BAE76178; BAE76178; BAE76178.
DR GeneID; 66671303; -.
DR GeneID; 945049; -.
DR KEGG; ecj:JW0388; -.
DR KEGG; eco:b0398; -.
DR PATRIC; fig|1411691.4.peg.1881; -.
DR EchoBASE; EB1086; -.
DR eggNOG; COG0420; Bacteria.
DR HOGENOM; CLU_038045_2_0_6; -.
DR InParanoid; P0AG76; -.
DR OMA; TSGNHDS; -.
DR PhylomeDB; P0AG76; -.
DR BioCyc; EcoCyc:EG11094-MON; -.
DR BioCyc; MetaCyc:EG11094-MON; -.
DR PRO; PR:P0AG76; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990391; C:DNA repair complex; IPI:ComplexPortal.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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 GO; GO:0006274; P:DNA replication termination; IBA:GO_Central.
DR CDD; cd00840; MPP_Mre11_N; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041796; Mre11_N.
DR InterPro; IPR004593; SbcD.
DR InterPro; IPR026843; SbcD_C.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF12320; SbcD_C; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR TIGRFAMs; TIGR00619; sbcd; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA recombination; DNA replication; Endonuclease;
KW Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..400
FT /note="Nuclease SbcCD subunit D"
FT /id="PRO_0000182195"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 21..37
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:6S6V"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 87..97
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 150..172
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 264..272
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 286..293
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:6S6V"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 320..327
FT /evidence="ECO:0007829|PDB:6S6V"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 342..347
FT /evidence="ECO:0007829|PDB:6S6V"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 362..372
FT /evidence="ECO:0007829|PDB:6S6V"
FT HELIX 379..388
FT /evidence="ECO:0007829|PDB:6S6V"
FT TURN 389..394
FT /evidence="ECO:0007829|PDB:6S6V"
SQ SEQUENCE 400 AA; 44714 MW; E8894089198C6D5B CRC64;
MRILHTSDWH LGQNFYSKSR EAEHQAFLDW LLETAQTHQV DAIIVAGDVF DTGSPPSYAR
TLYNRFVVNL QQTGCHLVVL AGNHDSVATL NESRDIMAFL NTTVVASAGH APQILPRRDG
TPGAVLCPIP FLRPRDIITS QAGLNGIEKQ QHLLAAITDY YQQHYADACK LRGDQPLPII
ATGHLTTVGA SKSDAVRDIY IGTLDAFPAQ NFPPADYIAL GHIHRAQIIG GMEHVRYCGS
PIPLSFDECG KSKYVHLVTF SNGKLESVEN LNVPVTQPMA VLKGDLASIT AQLEQWRDVS
QEPPVWLDIE ITTDEYLHDI QRKIQALTES LPVEVLLVRR SREQRERVLA SQQRETLSEL
SVEEVFNRRL ALEELDESQQ QRLQHLFTTT LHTLAGEHEA
