ID   RECC_BUCBP              Reviewed;        1111 AA.
AC   Q89AB4;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=bbp_403;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27115.1; -; Genomic_DNA.
DR   RefSeq; WP_011091516.1; NC_004545.1.
DR   AlphaFoldDB; Q89AB4; -.
DR   SMR; Q89AB4; -.
DR   STRING; 224915.bbp_403; -.
DR   PRIDE; Q89AB4; -.
DR   EnsemblBacteria; AAO27115; AAO27115; bbp_403.
DR   GeneID; 56470940; -.
DR   KEGG; bab:bbp_403; -.
DR   eggNOG; COG1330; Bacteria.
DR   HOGENOM; CLU_007513_0_0_6; -.
DR   OMA; SFDLMQY; -.
DR   OrthoDB; 1320159at2; -.
DR   Proteomes; UP000000601; 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; Reference proteome.
FT   CHAIN           1..1111
FT                   /note="RecBCD enzyme subunit RecC"
FT                   /id="PRO_0000087119"
SQ   SEQUENCE   1111 AA;  132960 MW;  A13BC72BC5A62FB1 CRC64;
     MFTLYKSLKF NLFVKSAFKV ILNEPLLNPL TKEIFIVNNK ETEQWIKIFI AKKYKVCTNI
     KFFKLKHFIL NILKQNTPKL YSKSEFSKYS IMWKIINIPD IQHLLTKIVS KNNTYSTLFK
     IASSISNLFQ LYLKYRPDYI KKWEQKSNIP KTRLKQKWQQ IIWMRIIKYT KDANKPILHF
     SNLLYDSIKK MQRNNFINTK LPVRIFIFNI TPITPQYAIF LKSISKYCSV HFFYATASYN
     DKQMFSTSFI KFKQTQEISN NQLLSLLHSK NKNIIYHEIE NFQKNTKFQS YWITYEYEQM
     LFLSLIKDKT INLNFKIKQN SLLQYLQNKI LNLHSIQKKN NEQENNKILI LKTDKSLSIH
     SCHTLIREIE VLHNNLLNIL NDNNDILFQD VLVISKNLDT YIPYINQIFN SASSKNFIPF
     SINYKNIKNI EFYKTILELI DLPNIELNIN KITNLLNIPT LLKKVQINEQ EIPILLQIIN
     QTEIQWENDN ILSNDWLSND ITKCWEHGLQ RIFLGQIINN IDYKFWENIV PYNEFSTLYY
     NIFNKLISLI SLLNKWKKIL SKPKFLSHWD ITFKKLLNDF FTDHEQKQPE AKLIIKKWTE
     IIHSGMQEKY TKKISITLLK NELCNSVSYI SQSNYLFSGK ITFCNNFTLT NIPFKIIYLI
     GLNDNISSNT HESFDIYNLL KLHPRAYDPC DEINHKNLLL KTLLSAKKFF YISHQIVSNN
     YKKLNNIPIA IDKIIKYITQ YFYIKNKNKD NFNDNLKDIK SHIYHNYTFY AHEKRNFLEK
     LNYPNFNTTI WKMATLINNS HKEFIKKLPS IKNQTINYNT LILFWKNPIQ TFFHVRLNIQ
     LNTTKNKHMH QNKHFINKLD QYKMNKTLLK FFLYKQNTNQ LFQYYKNIGI IPNNNIGNII
     WEYTKKLITP LYDQIMKIKK ILNNSKFCIN VKNKCMLHGQ LKNINSSGGL LRWKATKLSF
     QDIISCWLEH LLYCSLYKKH NSILIGTNHQ IITFYKLENK TAKYYLKKYI SGYFDGMEQP
     ILLTKSGINW INAIYDKKNN KFYTNTNKNL NAYKIFLNTW NGNNWITGEK DDPYIQKMIV
     YLTKKNIQKI YKTTKKWLTP ILKNISYSKY H