ID   SBCC_RHOCB              Reviewed;        1238 AA.
AC   O68032; D5AV82;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Nuclease SbcCD subunit C;
GN   Name=sbcC; OrderedLocusNames=RCAP_rcc02134;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=9256491; DOI=10.1073/pnas.94.17.9384;
RA   Vlcek C., Paces V., Maltsev N., Paces J., Haselkorn R., Fonstein M.;
RT   "Sequence of a 189-kb segment of the chromosome of Rhodobacter capsulatus
RT   SB1003.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:9384-9388(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
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; AF010496; AAC16118.1; -; Genomic_DNA.
DR   EMBL; CP001312; ADE85864.1; -; Genomic_DNA.
DR   PIR; T03465; T03465.
DR   RefSeq; WP_013067843.1; NC_014034.1.
DR   AlphaFoldDB; O68032; -.
DR   SMR; O68032; -.
DR   STRING; 272942.RCAP_rcc02134; -.
DR   EnsemblBacteria; ADE85864; ADE85864; RCAP_rcc02134.
DR   GeneID; 31490985; -.
DR   KEGG; rcp:RCAP_rcc02134; -.
DR   eggNOG; COG0419; Bacteria.
DR   HOGENOM; CLU_004785_1_1_5; -.
DR   OMA; ISHVQEM; -.
DR   OrthoDB; 1143316at2; -.
DR   Proteomes; UP000002361; 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..1238
FT                   /note="Nuclease SbcCD subunit C"
FT                   /id="PRO_0000105867"
FT   REGION          661..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          395..438
FT                   /evidence="ECO:0000255"
FT   COILED          466..487
FT                   /evidence="ECO:0000255"
FT   COILED          521..600
FT                   /evidence="ECO:0000255"
FT   COILED          724..770
FT                   /evidence="ECO:0000255"
FT   COILED          901..943
FT                   /evidence="ECO:0000255"
FT   COILED          1019..1052
FT                   /evidence="ECO:0000255"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1238 AA;  128048 MW;  2B6BC6C63A859AE1 CRC64;
     MRILSISGQN IASLAAPFRI DFTTAPLAGA GLFAITGETG AGKSSILDAM CLALYGDAPR
     LSAGARSDKV PDAAGEEISA ADSRAILRRG AATGWAEVRF AGRDGLEYIA RWQARRARDK
     VEGKLQTVAR SLARAEDGQV LAAQTQAVSE QVAALTGLSY EEFRRTVLLA QGDFDAFLRA
     DTGERATLLE KVTGTGLYRA VSIRVYERTE MARAEHAQLL ARAAEHRLLD DAARAALTEE
     IAARTAATAA ATAERAGLSE ALARHRRHAE AVRQVQAAAA ALAGAEALQA EAGPARAQLD
     RLERAAPLHL PWQAAAEARA RLDAARSGAE AAAASRSLAA QALATRADAA ARATAAGTET
     EEAFKAFGRI WDRAAALDAQ IATAATEAEA ARTRAAETAR AAAGIRRAEA DLAAAETRAQ
     QARQAAEARL AELAAQAPLA DDWPQLRRDL ADHRAACAAQ AAAATAAQAA QDRAQALAQE
     ARAAAAAEAR DQAADSALAK AAAALQQALA PLEAAHPPAR TADLARIETD LAELTRALRD
     GAEAAALGAA AQRAATAAAT EAALARAQES AAKQDLDRAE TQIAALTAPL EQADLALSDA
     ARSLRAQLSA GSPCPVCGAL EHPTPAEAGL AHLAERLRAD QAAARGAAQA ARDALTAAQG
     ARATAEARGT QAAEDQRRAQ TRAEAARAAW GDTQPRVSAR PLAPALPGTP DPTALAAAQD
     RLCALQTAEA AAQAEISALR TRLTEAERDR ERLRRALLAH RGTRERLAVQ QAETAQEAAL
     AEARRTEAAA RRDGLALALA PALARAGEDD PAAPGLAERL AATVSAVGAA RTGLQAAQEA
     LSALAPQLAA ARRDSETATA QAQSAAQAAR DRDGAWAALR AERAPLLDGQ PTALHRSRFN
     DQRLAAQRAQ QAAAADLATA QAALAAAEAR AAETARAASE AATAQRAAEA DLAAALEAAA
     MSAAELAALI ALPPGTAERL RADLRGRDDA VTAARSALGA RKTDLQEIED QGNPAEDPEA
     LSARLAALEA EAERRAQEIG QLSAELARDA ATRAALAGLA VETEAARAEL EVWEAVNKAI
     GARSGDRFAR IAQAITLDVL VEHANRHLAD LNPRYRLRRA AELSLQVEDR DMGDTARATR
     SLSGGERFLV SLALALALSQ MGGKGTFAGT LFIDEGFGAL DAGSLDLAID ALETLQSQGR
     QVGVISHVEA MQARIATRIA VRKEGGGRSS LRVEGPGV