ID   SBCC_TREPA              Reviewed;        1047 AA.
AC   O83635;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Nuclease SbcCD subunit C;
GN   Name=sbcC; OrderedLocusNames=TP_0627;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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; AE000520; AAC65599.1; -; Genomic_DNA.
DR   PIR; D71302; D71302.
DR   RefSeq; WP_010882073.1; NC_021490.2.
DR   AlphaFoldDB; O83635; -.
DR   IntAct; O83635; 2.
DR   STRING; 243276.TPANIC_0627; -.
DR   PRIDE; O83635; -.
DR   EnsemblBacteria; AAC65599; AAC65599; TP_0627.
DR   KEGG; tpa:TP_0627; -.
DR   eggNOG; COG0419; Bacteria.
DR   HOGENOM; CLU_004785_2_1_12; -.
DR   OMA; ISHVQEM; -.
DR   OrthoDB; 1143316at2; -.
DR   Proteomes; UP000000811; 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   InterPro; IPR004592; SbcC_gammaproteobac_type.
DR   Pfam; PF13476; AAA_23; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00618; sbcc; 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..1047
FT                   /note="Nuclease SbcCD subunit C"
FT                   /id="PRO_0000105868"
FT   COILED          178..276
FT                   /evidence="ECO:0000255"
FT   COILED          305..332
FT                   /evidence="ECO:0000255"
FT   COILED          382..410
FT                   /evidence="ECO:0000255"
FT   COILED          521..547
FT                   /evidence="ECO:0000255"
FT   COILED          624..667
FT                   /evidence="ECO:0000255"
FT   COILED          698..729
FT                   /evidence="ECO:0000255"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1047 AA;  118647 MW;  D900680131EA3F5D CRC64;
     MKPMRLTLHN IGPFVGTHTV DFTALGPIFL VCGKTGSGKT TLFDAIAYAL YGKPLGTRAE
     VIRSLRSHYA APSEAAFATL EFSLGTKIYR VHRTLTCTLS HRKTEQPEQL YLEQKKGHGW
     ERIACAHKSE TECVIHDLLK LNSKEFERVV MLPQGECAQF LKANSKEKKE TLMNLFPVDQ
     YTALMERAKK KSLHAKAVLE TLRSQLETLC AECMPDTYHE RKQTLEAELQ HARDALQQTR
     ISHAYYTQKR EALEAQLKKQ QLCKELRARI ETYRAQEPVH AETQKRIDRA RKAAPLAAHI
     KHVTQCEQDA QRIHAEIQEK MRSREQLLMK RAAHVAQQSS IEEQRRLLQT LHSACIHIED
     AHDVATSIRD ISCQAHTLTQ HIHTLAQQKT TLTQQEQSLC KELDILQREA GTIDTRTSAF
     NDLQIQLAHA KKTQELSQRY AELCAAHATC TAQCEKLEKI HAQKSAYSTR AREQLLQTKE
     QIHLQETRTH AVVLARLLEH QEPCPVCGSC IHPNPARQDI DNLEPLTRRM QRIEQTYAQL
     ETSEKDVYHI LTSERERRAS YSAQMQEIQH SFSILTSCDT RSSCDIPNVQ KITVRVLDLT
     EKLSRAKDML ACAQHALLRK KQPEQDLQDV RAHLQQCSQE LAKKETALHA LQETLTQQRV
     RIHALSIRLP KELLASNLLA PQKMQHEKES VAYWKEMLAH CQTLMRELHT HIEEYDREFN
     EIENASSALG ADIAAREDAL NHVQKEYMHL ARTVCCARTE AHFNNNEEVT AALMTDAELS
     HAAAEIQFFN ELRAADTHLL KTLEAEIGTE IPSDLDELNA QCHTLVKDEE NFLSRIEILS
     ATLHTLTHQY LKYEECSKQL AQKTQESAKL ITLSDELNGI NQKKIQFDAW ALISFLHEIT
     AYANIRLQKM SEGRYHLRVA DSHVNARGYQ GLALLVADAY TGSVRPSATL SGGETFMASI
     SLALGLADSI QTRSGGIVLD SLFIDEGFGS LDEASLDKAI GILDEIREGS RMIGIISHVH
     ELRTRIPHKI LIKKTNAGSH VMQGDAE