ID F4TAQ2_ECOLX Unreviewed; 1047 AA.
AC F4TAQ2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Nuclease SbcCD subunit C {ECO:0000256|RuleBase:RU363070};
GN Name=sbcC {ECO:0000256|RuleBase:RU363070};
GN ORFNames=ECJG_04060 {ECO:0000313|EMBL:EGI23118.1};
OS Escherichia coli M718.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=656419 {ECO:0000313|EMBL:EGI23118.1, ECO:0000313|Proteomes:UP000002790};
RN [1] {ECO:0000313|EMBL:EGI23118.1, ECO:0000313|Proteomes:UP000002790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M718 {ECO:0000313|EMBL:EGI23118.1,
RC ECO:0000313|Proteomes:UP000002790};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Escherichia coli M718.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|RuleBase:RU363070}.
CC -!- SUBUNIT: Heterodimer of SbcC and SbcD. {ECO:0000256|RuleBase:RU363070}.
CC -!- SIMILARITY: Belongs to the SMC family. SbcC subfamily.
CC {ECO:0000256|RuleBase:RU363070}.
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DR EMBL; GL884105; EGI23118.1; -; Genomic_DNA.
DR RefSeq; WP_000698913.1; NZ_GL884105.1.
DR AlphaFoldDB; F4TAQ2; -.
DR HOGENOM; CLU_004785_1_0_6; -.
DR Proteomes; UP000002790; Unassembled WGS sequence.
DR GO; GO:0016887; F:ATP hydrolysis 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 GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR004592; SbcC_gammaproteobac_type.
DR NCBIfam; TIGR00618; sbcc; 1.
DR PANTHER; PTHR32114; ABC TRANSPORTER ABCH.3; 1.
DR PANTHER; PTHR32114:SF2; ABC TRANSPORTER ABCH.3; 1.
DR Pfam; PF13476; AAA_23; 1.
DR Pfam; PF13558; SbcC_Walker_B; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|RuleBase:RU363070};
KW DNA recombination {ECO:0000256|RuleBase:RU363070};
KW DNA replication {ECO:0000256|RuleBase:RU363070};
KW Endonuclease {ECO:0000256|RuleBase:RU363070};
KW Exonuclease {ECO:0000256|RuleBase:RU363070, ECO:0000313|EMBL:EGI23118.1};
KW Hydrolase {ECO:0000256|RuleBase:RU363070};
KW Nuclease {ECO:0000256|RuleBase:RU363070}.
FT DOMAIN 5..206
FT /note="Rad50/SbcC-type AAA"
FT /evidence="ECO:0000259|Pfam:PF13476"
FT REGION 837..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 238..354
FT /evidence="ECO:0000256|RuleBase:RU363070"
FT COILED 539..580
FT /evidence="ECO:0000256|RuleBase:RU363070"
FT COILED 618..645
FT /evidence="ECO:0000256|RuleBase:RU363070"
FT COILED 772..806
FT /evidence="ECO:0000256|RuleBase:RU363070"
SQ SEQUENCE 1047 AA; 118498 MW; 17C3FF2F316A6C6D CRC64;
MKILSLRLKN LNSLKGEWKI DFTREPFASN GLFAITGPTG AGKTTLLDAI CLALYHETPR
LSNVSQSQND LMTRDTAECL AEVEFEVKGE AYRAFWSQNR ARNQPDGNLQ VPRVELARCA
DGKILADKVK DKLELTATLT GLDYGRFTRS MLLSQGQFAA FLNAKPKERA ELLEELTGTE
IYGQISAMVF EQHKSARTEL EKLQAQASGV ALLTPEQVQS LTASLQVLTD EEKQLLTAQQ
QEQQSLNWLT RLDELQQEAS RRQQALQQAL AEEEKAQPQL AALSLAQPAR NLRPHWERIA
EHSAALAHTR QQIEEVNTRL QSTMALRASI RHHAAKQSAE LQQQQQSLNT WLQEHDRFRQ
WNNELAGWRA QFSQQTSDRE HLRQWQQQLT HAEQKLNTLA AITLTLTADE VASALAQHAE
QRPLRQRLVA LHGQIVPQQK RLAQLMVTIQ NVTLEQTQRN AALNEMRQRY KEKTQQLADV
KTICEQEARI KTLEAQRAQL QAGQPCPLCG STSHPAVEAY QALEPGVNQA RLLTLEKEVK
KLGEEGAALR GQLDALTKQL QRDENEAQSL RQDEQALTQQ WQAVTASLNI TLQPQDDIQP
WLDAQDEHER QLRLLSQRHE LQGQIAAHNQ QIIQYQQQIE QRQQQLLTAL AGYALTVPQE
DEEESWLATR QQEAQSWQHR QNELTALQNR IHQLTPILET LPQSDELPHS EETVVLENWR
QVHEQCLALH SQQQTLQQQD VLAAQSLQKA QAQFDTALQA SVFDDQQAFL AALMDEQTLT
QLEQLKQNLE NQRRQAQTLV TQTAETLAQH QQHRPGGLAL TVTVEQIQQE LAQTHQKLRE
NTTSQGEIRQ QLKQDADNRQ QQQTLLQQIA QMTQQVEDWG YLNSLIGSKE GDKFRKFAQG
LTLDNLVHLA NQQLTRLHGR YLLQRKASEA LEVEVVDTWQ ADAVRDTRTL SGGESFLVSL
ALALALSDLV SHKTRIDSLF LDEGFGTLDS ETLDTALDAL DALNASGKTI GVISHVEAMK
ERIPVQIKVK KINGLGYSKL ESTFAVK
//
