ID   RECC_HAEIN              Reviewed;        1121 AA.
AC   P44945;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=HI_0942;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC22596.1; -; Genomic_DNA.
DR   PIR; G64103; G64103.
DR   RefSeq; NP_439102.1; NC_000907.1.
DR   RefSeq; WP_005693290.1; NC_000907.1.
DR   AlphaFoldDB; P44945; -.
DR   SMR; P44945; -.
DR   STRING; 71421.HI_0942; -.
DR   PRIDE; P44945; -.
DR   EnsemblBacteria; AAC22596; AAC22596; HI_0942.
DR   KEGG; hin:HI_0942; -.
DR   PATRIC; fig|71421.8.peg.983; -.
DR   eggNOG; COG1330; Bacteria.
DR   HOGENOM; CLU_007513_0_0_6; -.
DR   OMA; SFDLMQY; -.
DR   PhylomeDB; P44945; -.
DR   BioCyc; HINF71421:G1GJ1-982-MON; -.
DR   Proteomes; UP000000579; 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:0006310; P:DNA recombination; IBA:GO_Central.
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.
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..1121
FT                   /note="RecBCD enzyme subunit RecC"
FT                   /id="PRO_0000087121"
SQ   SEQUENCE   1121 AA;  129669 MW;  E5070957296AE0D3 CRC64;
     MFIVYYSNQL EKQKEILSSL FKSLPPEDPF QQDIILVQSP NMAQWLQIEL AKETGISANL
     KFPMPASFIW QLYAQNLPAT ALENPFDKDS MMWRLMRLIP IFLEKENFSP LRNYLSSSPH
     SEQYKLYQLS SKIADLFDQY LVYRPEWIFA WEKGEDEQIT DQIQKQQPNL NATLFAQIQG
     NTKWQGELWR ALVVDVKSDV NEATHRAALH NQFLALLADK KAPKKLPSRI FIFGIPALPT
     AYLNILQAIS SEVDIHLFFN NPCQEYWGDI SDLRLDYLRS RQRYQFNKQD ENQPLFSEDQ
     LSQLENAQFD VTYQKENLQL GNPLLAAWGK MGRDFLYILV RDEEHIPTYP VNAYQEIESN
     SLLGQLQSQI LHLENKPLNI AKNDRTLTLH SCHSAMREVE VLHDYLLDLF NQDPSLTPKD
     VVVMVADINQ YTPYIQAVFG QKNGDVPQIP FSLSDNKLSE SDVLVSSYLT LLRLKESNFS
     AEDVLVLLDI PAMRERFNIS LADLPLVREW VTDSGIRFGL QKNQDGINFN SWQAGLERMI
     LGYAMREEQG IWQDSLGLNS SYGLKGELAG NLSHFFTALS ALHETLQQAH SIEKWQEILT
     ALLSDFFVRN EDTSDMIFYI QEKINELAEH LKTLHFNEEL QAEVIADVIT MQLEDAPNSL
     KFLAGKVNFC TLLPMRSVPF KVVCLLGMND ADYPRTQTPN SFDLMQYHYQ KGDRVRRDDD
     RYLFLEALLA ARDYCYISYV GRSITDNQPK EPSVLVSQLL DYINQGQKEN VLTVIEHPMT
     AFSPDNFKNN EKFTRSFATK WLPIAQFDAS SNNSEFAVTM TENLEKIEEV ELDALVSFVE
     NPVKFFFEKQ LGVYFRDKDE RIADSENFTL SGLDNYSLNN DLIYLDEQNF ADYFRQAEVK
     GVLPRAEFGK VYAENIRDNV LEFKKKIADL GEAKHASVDF NLSVDWQNEN QKIRLFGYMD
     ALFGDDSQVI HWHFAKYKDR YCIRPWIYYL IQCVTQENAV PAKLITQDKV LELPPIEREV
     ALAQLQIYVK DYLQSQIEIQ LVPTVRNISD FIVSDENSVS EKLQELTESN GFGPKADPYW
     SRVLAQTSRF KQPENIAKLL KQTKAWFGLL FAQKKTRKTQ S