ID A1BGA4_CHLPD Unreviewed; 1077 AA.
AC A1BGA4;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=RecBCD enzyme subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
DE EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01486};
DE AltName: Full=Exonuclease V subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
DE Short=ExoV subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
DE AltName: Full=Helicase/nuclease RecBCD subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
GN Name=recC {ECO:0000256|HAMAP-Rule:MF_01486};
GN OrderedLocusNames=Cpha266_1402 {ECO:0000313|EMBL:ABL65431.1};
OS Chlorobium phaeobacteroides (strain DSM 266 / SMG 266 / 2430).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290317 {ECO:0000313|EMBL:ABL65431.1, ECO:0000313|Proteomes:UP000008701};
RN [1] {ECO:0000313|EMBL:ABL65431.1, ECO:0000313|Proteomes:UP000008701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 266 {ECO:0000313|EMBL:ABL65431.1,
RC ECO:0000313|Proteomes:UP000008701};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_01486};
CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01486}.
CC -!- SIMILARITY: Belongs to the RecC family. {ECO:0000256|HAMAP-
CC Rule:MF_01486}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000492; ABL65431.1; -; Genomic_DNA.
DR RefSeq; WP_011745247.1; NC_008639.1.
DR AlphaFoldDB; A1BGA4; -.
DR STRING; 290317.Cpha266_1402; -.
DR KEGG; cph:Cpha266_1402; -.
DR eggNOG; COG1330; Bacteria.
DR HOGENOM; CLU_007513_0_0_10; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000008701; 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 CDD; cd22353; RecC_C-like; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 1.10.10.990; -; 1.
DR Gene3D; 3.40.50.10930; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01450; recC; 1.
DR PANTHER; PTHR30591; RECBCD ENZYME SUBUNIT RECC; 1.
DR PANTHER; PTHR30591:SF1; RECBCD ENZYME SUBUNIT RECC; 1.
DR Pfam; PF04257; Exonuc_V_gamma; 1.
DR Pfam; PF17946; RecC_C; 1.
DR PIRSF; PIRSF000980; RecC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01486, ECO:0000313|EMBL:ABL65431.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01486};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01486};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01486}; Reference proteome {ECO:0000313|Proteomes:UP000008701}.
FT DOMAIN 794..1013
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
FT REGION 311..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1077 AA; 121429 MW; 8B8CC7D31BF86A21 CRC64;
MTLHLYTGNR METLVDALAE VLGRNPPSVF EYEKIVVQSR GMQRWISMEL ARRFGVWAGA
EYPFPNRLLQ QLFEEMELTQ PDSSTFSKEV MCWSMMRLLP EMLDRELFSP LRSYLRNDRD
GLKLFQLSGR IADTFDQYTL FRTDLLAAWE EGRDDGARDW QPELWRALVA ESSGKHRGRL
KTEFCLKVRH ASLPAGFPKR ISLFGISYMP PYHIGMIEAL ATRIPVNIFL LSPTQEYWSD
IVSRRKLFRM SEGERELSTE GNPLLASLGR SGREFADLLL EAGGIENEHD LYIEPADDTL
LHALQSDMLN LSGTGEEGER RPAPERADRS VQVHSCHNPL REVEVLHDNL LDLLERLPGL
EPREIVVMTP EIETYAPYIA TVFGSSGDGV SRLPHSIADR RMLDEGGIAP ALLKLLELYG
SRLPSPDIFD LLSSPPVSRR FRLDEEELDT IRVWVADTRI RWGMDERSRS GLGLPPFRDN
SWRAGLERLL LGYAMPDEGV LFDGVLPFDV EGDAETLGKF ADFIDALEAL SARFDRPRTL
DGWRDHFIWM LDIFIDADEE VERELSHIAA EIDKLTELAG EASFGGETAA PVMIAWLRGR
LEKFEMGLGF MTGGITFCAM LPMRSIPFRV VAMIGMNDGA FPRQQRLPGF DMMSREPRKG
DRSVRGDDRY LFLESILSAR DVLYLSYVGQ SIRDNSEQPP SVLVSELLDA IERGFAFSEG
EDAISRMVVR HKLQGFNPAY FTERSPLFSY SDDNFRALAC RDERNAGNGS RGRNPVEARP
FMDEPLPEAD DGDRRVTIDD LVKFFANPSA FFLDRQLGLK PSAALRPLEE REPFGAEGLD
AYMMRQELLA AVLEGGKEEA LLPLFRSRGL LPPARHGELL FGELLAEVRE FADRLPELKG
SAAPAVLEAD LDIGGFRLTG RLDHLLPSGQ LLYRCAKMRE KDRIGSWILH LVLGACSPGH
MQETRLVMLD RAVRYTPVAD ASGRLETMLS LYRQGLLEPL PFFPRASTAW AGKAEKTERE
RIEAALAAWR EGYGGREGEG ADPAFRRCFG TEPPLGERFA AITEEVLLPM LEHGGKG
//
