ID   RECC_BUCAP              Reviewed;        1061 AA.
AC   Q8K9B0;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=RecBCD enzyme subunit RecC {ECO:0000255|HAMAP-Rule:MF_01486};
DE            EC=3.1.11.5 {ECO:0000255|HAMAP-Rule:MF_01486};
DE   AltName: Full=Exonuclease V subunit RecC {ECO:0000255|HAMAP-Rule:MF_01486};
DE            Short=ExoV subunit RecC {ECO:0000255|HAMAP-Rule:MF_01486};
DE   AltName: Full=Helicase/nuclease RecBCD subunit RecC {ECO:0000255|HAMAP-Rule:MF_01486};
GN   Name=recC {ECO:0000255|HAMAP-Rule:MF_01486}; OrderedLocusNames=BUsg_438;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for
CC       recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly
CC       rapid and processive ATP-dependent bidirectional helicase activity.
CC       Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator)
CC       sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the
CC       Chi site. The properties and activities of the enzyme are changed at
CC       Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and
CC       facilitates RecA-binding to the ssDNA for homologous DNA recombination
CC       and repair. Holoenzyme degrades any linearized DNA that is unable to
CC       undergo homologous recombination. In the holoenzyme this subunit
CC       recognizes the wild-type Chi sequence, and when added to isolated RecB
CC       increases its ATP-dependent helicase processivity. {ECO:0000255|HAMAP-
CC       Rule:MF_01486}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage (in the presence of ATP) in either
CC         5'- to 3'- or 3'- to 5'-direction to yield 5'-
CC         phosphooligonucleotides.; EC=3.1.11.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01486};
CC   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC       to DNA-binding. {ECO:0000255|HAMAP-Rule:MF_01486}.
CC   -!- SIMILARITY: Belongs to the RecC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01486}.
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DR   EMBL; AE013218; AAM67981.1; -; Genomic_DNA.
DR   RefSeq; WP_011053948.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9B0; -.
DR   SMR; Q8K9B0; -.
DR   STRING; 198804.BUsg_438; -.
DR   EnsemblBacteria; AAM67981; AAM67981; BUsg_438.
DR   KEGG; bas:BUsg_438; -.
DR   eggNOG; COG1330; Bacteria.
DR   HOGENOM; CLU_007513_0_0_6; -.
DR   OMA; SFDLMQY; -.
DR   OrthoDB; 1320159at2; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_01486; RecC; 1.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006697; RecC.
DR   InterPro; IPR041500; RecC_C.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   Pfam; PF17946; RecC_C; 1.
DR   PIRSF; PIRSF000980; RecC; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF52980; SSF52980; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW   Hydrolase; Nuclease; Nucleotide-binding.
FT   CHAIN           1..1061
FT                   /note="RecBCD enzyme subunit RecC"
FT                   /id="PRO_0000087118"
SQ   SEQUENCE   1061 AA;  127631 MW;  D0A2AB7F58E9EF5C CRC64;
     MFFVYRSNQI DILFTKICKI IKKKPLLNIF EREIIIHDNE ILFQNLNTFI ANHTGIAADF
     KLIYPNVFIW KLFKQVFSDI QLNNIFSRST ITWKIMKIIE ENDFCKFVQK KDKIMKKFEF
     SFLMSHLYQQ YILYRPNWIN MWEKNKKNTL KIEKKDEWQA KLWIKIILYT EKLQQSKWHF
     SNLFKKFKTL KKIEHIKFPK RIFIIYSISL NPKYMEIFKK ISTYTDIYFL SINACEKKIF
     HISFAKNYVV QKNNLLMNLS EKYEKFYFLF FKKFKKIKYN NFFQKNNSNN LLNIVKNDFL
     NFKEKENLLK KNSFLLKDNS ISINICCDKK HEIEVLYNKL LSFFNEDSKL KPSDIVITSF
     SLNTYIIYIN SIFKSKNKKE KIPFYISKKH SDKIEKILFI FNKILNLPNI RCNNEEILDL
     IEIQDIRDKF DISEEEINIL YEWIEKANIR WGLHENEKQK NNLIFIKKNQ NTWFYGIKKL
     LISHAINEEE EVWNNVLSCT SINTSRTELI GKLINFIKVL DQWRDKLFFS KKIKSWRPLF
     LCFIKDFFYK NEKIRDSIDI INKTWTKMID DATLSNYEKK IPISILKKKF SHIMNNFSEK
     KFLPGVINFC HPSLVCYIPF KIKCIIGAEY QEIPKKKLSS FNLIDKYPLT SDLHICKENY
     IFLQNFISTQ ETLYISYVGH SLKNNNKVRS SILIDQLLNH ITSNFYVSEH HDYKNNKKEI
     FEHICKKHKK ENLYEKKQVN KINLNTLQKT KKINQEIYNK IFSIKNRIIS TSTQISLKSL
     ISFWKNPIRY FFNYTLNIKL KIAKRNIITE PFSINLFDDF KISNIIFKKI LNNESIKDEF
     KKIILSGILP YGHFGSILLK EKKKEIENIV KAIYKYRISS PKKENFDIKI EKYNINGCLD
     EIQNTGLLRW KLGTINYRDR ISLWLEHLIY CILGGTGESK IIGYKKNFFS FYPLSSHLAY
     NYLFTYIEGY MKGMKNPLLL IKSGSNWFDK VYDKKNDCIK KNDDIKRKAY KILYHTWMGN
     EYITGEKEDL YIQQIISELN VKKICKISQK WFTPILKHQK K