ID A0A1B2LW53_9GAMM Unreviewed; 1240 AA.
AC A0A1B2LW53;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=BFG52_01580 {ECO:0000313|EMBL:AOA57170.1};
OS Acinetobacter larvae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1789224 {ECO:0000313|EMBL:AOA57170.1, ECO:0000313|Proteomes:UP000093391};
RN [1] {ECO:0000313|EMBL:AOA57170.1, ECO:0000313|Proteomes:UP000093391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRTC-1 {ECO:0000313|EMBL:AOA57170.1,
RC ECO:0000313|Proteomes:UP000093391};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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}.
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DR EMBL; CP016895; AOA57170.1; -; Genomic_DNA.
DR RefSeq; WP_067551700.1; NZ_CP016895.1.
DR AlphaFoldDB; A0A1B2LW53; -.
DR STRING; 1789224.BFG52_01580; -.
DR KEGG; ala:BFG52_01580; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000093391; 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; 3.40.50.10930; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01486; RecC; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006697; RecC.
DR InterPro; IPR041500; RecC_C.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
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}; Helicase {ECO:0000256|HAMAP-Rule:MF_01486};
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:UP000093391}.
FT DOMAIN 934..1152
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1240 AA; 141924 MW; 3C5636115F013C29 CRC64;
MGIHVIQSQR LDILLQGVLH TTQQQSTDPF AILASQHIVA PSTAIQEWLT LRLSEAQGIS
ANSIFHQRIR GLQWYLYQQV LTDKERVRKA NIPSLVLKWR IYQVLLEQFQ QYAKQNAKQT
EKQTSSSAQA SNPHPLSSLL QRVIDNGKAL PSAKQQRQRQ HAMLYWIAEQ LAQLFTHYMV
YRGECQADCP TGQCRCRGNW LAAWSRDQAL NVEQLLNVSE HADAAYQLEQ AQQLEAWQRW
LWQQGFAQDF AEILAVDQAF WATLDDPQQR NDALAQLPAQ VVVFTLLELP PNQLKFLRRL
GQYIDVYILH YNPSQEYWAD SVDPLWKKQY DLGVKQRYLQ QHPQASAAEL AAFFQDFTLN
FNALVRESRH PLLTRFGKQA RDHFSLLAQL SAGVEGQWVD AFVQFPITNL LSKIQSDILN
LTEPEAGAYL LATDDQSIQI HVCHSTLRQL EVLKEQLLHW LAQGTAEQPR RPSDIVVMVP
QLASLEALIR SVFPQQVQKD GIYLPVKIAG ISSLDAQHAW RAVLGRFCWV EQRFNIEEFT
DWLQLAATQQ YYALDSDATA RILVLLQQAG FRRGLDAEHL QLSLDASDQD YRYSFQFALN
RLVMGIAIPE RVVCNEILSF EQVYQDDFAL IDILIRIYQD FSTRRNALHA HLQAEHMPDV
EYWLRYLLEE VEAFEQAGVT ALAPIKEILH KQQRMLTLAQ FYAQDQQGLT RTFQLPLSDV
LMEVEKALLH QADQVLPTGQ ITFCEIGQIR PIPYQLVVLL DLDAGVFPNR QQHTAFDLMD
LLKAQLGDRS RLEDDQGAFL DALLLAEQGL WLFYNGFDVN DAEARDPSSV LQELIQHFSL
ICAMPEATPA DVIPTDAMIE KDGIVIAANI QQLYQVHPLQ PFDPNGFIQQ QPVRFQDHWY
QVAAQLQKLR GVQRQIYWND VAAPIVLNET ASYIDARQWI QAMCFPVQWY LQQLGVQNPS
AMTVLPEQEP LLLDGLGRYA LRDFMVQHQQ PEALALPLLQ DQLPVGKIQH SAWQMSQAEH
SLLMQRLQRY GAAPTQTTPR YWQASPTYRF QIELPAAGQS TWLSLDAASA RGKRRAKVWL
EYLFWLAASD LAADQGTDWQ RIAVFSDVTL QCCGLSQQQA QAYLQQWLAA STQAAQQVLV
LPAALLLSAA EKNKALHWQQ DAQGHWQLAE WDDLRKQWQG DQAHFGAGPA AEDNEACRLH
RDWQFVLQEQ DSTALLDAAC QQYSYALYAP IYQHQRVIEE
//
