ID   RECC_BUCAI              Reviewed;        1070 AA.
AC   P57528;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=BU453;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13151.1; -; Genomic_DNA.
DR   RefSeq; NP_240265.1; NC_002528.1.
DR   RefSeq; WP_010896125.1; NC_002528.1.
DR   AlphaFoldDB; P57528; -.
DR   SMR; P57528; -.
DR   STRING; 107806.10039117; -.
DR   PRIDE; P57528; -.
DR   EnsemblBacteria; BAB13151; BAB13151; BAB13151.
DR   KEGG; buc:BU453; -.
DR   PATRIC; fig|107806.10.peg.463; -.
DR   eggNOG; COG1330; Bacteria.
DR   HOGENOM; CLU_007513_0_0_6; -.
DR   OMA; SFDLMQY; -.
DR   Proteomes; UP000001806; 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; -; 1.
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.
DR   TIGRFAMs; TIGR01450; recC; 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..1070
FT                   /note="RecBCD enzyme subunit RecC"
FT                   /id="PRO_0000087117"
SQ   SEQUENCE   1070 AA;  128579 MW;  8F644C84877981AF CRC64;
     MFTIYKSNSL NTLLLKAYHI IEEKPFSNIF EKEIFIYDNK VLFQYLNIFI AEKKGISANF
     KFYHPNDFIW KLFKIILSKK ELKNIFTHSM IIWEIIKILD NKKFFENCSK KKDMIKKFKF
     SFLMASIFKK YILYRPEWIN QWEIEKNISI FDKNEQWQIK LWMEIIHNTK KINQSSDHFA
     NLFYNIQKII KEKKIKKKYL PKRFFIISSF SMNPSYIKIF QNISIYTDIY FLYITPFKKN
     IFNFIQDNKI FTDIKIEKKN ILNDSLITLW GQYEEIYYFY ILKSKKNKVI NCFKKNKNKS
     LLSQIKNNFF NDSEFTRKKR FLEISDHSIS INICFNKKNE IEVLYEKLLI FLNENSSIKP
     GDIVVTSFSL DTYISSINLI FQSIDNKKTI PFFIAKKSSK TTEIMLWSFK KILNLSNSRF
     ENEEILELLD VPEIAEKFNF SEEEIKILYH WIEETNIRWG INEKHKNYLL FPKNKQNTWF
     YGIEKLLLSY AMNDTEKIWN GVLSCSFING SRSELIGKLI SFIKILEKWQ KKLSKLQYLT
     YWRSLYSDLV SDFFQNNTKI EKSIQIIQKK WIEIIDDSLS SNYLKKISIN ILKKIFFYKY
     YDNNHEIFLP GVVNFCYPDS VCYIPFKVIC MIGTDHTSIP KTNYLDNFNL LKKYPLIGDI
     NLYQKYSYLF VQSLSCAEKY FYISYIGYSV KDESKVHPSI LVDQLLNYIT LNFCFIGDQN
     LSYKENSKKI TKYLCKKHKK QFFYETKNIE SFIQDDIKND FKHTEKNISH KNLLKKNTDN
     EINLKDLINF WKHPIRYFYN SHLKIKIRQK KQKINTTETF LVNPLNSFKI KNKLLDYIIH
     NKNITKLYQH YLLSGKLPYH FFGEIFWIKN IKEMKLIANK VMQYRIEKEE KKINLNIEKY
     QIYGVLSEIQ STGLLRWKTS SIRYSDRIAL WLEHLIYSIL GGCGKSKIIG YKSQIWSFSS
     LNSHRAHSYL LEYIKGYIKG MKEPLFLTKS GASWLDQVYD ERNNCIKNDY YTKIKAYKKL
     LYTWKGDNYT EGEQEDYYLK KTITISNKKN IKKICESAEK WLIPILKNKG