ID A0A0N9WCI0_9GAMM Unreviewed; 1230 AA.
AC A0A0N9WCI0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=AOY20_05660 {ECO:0000313|EMBL:ALH95064.1};
OS Acinetobacter equi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1324350 {ECO:0000313|EMBL:ALH95064.1, ECO:0000313|Proteomes:UP000064939};
RN [1] {ECO:0000313|EMBL:ALH95064.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114 {ECO:0000313|EMBL:ALH95064.1};
RX PubMed=26620413;
RA Poppel M.T., Skiebe E., Laue M., Bergmann H., Ebersberger I., Garn T.,
RA Fruth A., Baumgardt S., Busse H.J., Wilharm G.;
RT "Acinetobacter equi sp. nov. isolated from horse faeces.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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; CP012808; ALH95064.1; -; Genomic_DNA.
DR RefSeq; WP_054580962.1; NZ_CP012808.1.
DR AlphaFoldDB; A0A0N9WCI0; -.
DR STRING; 1324350.AOY20_05660; -.
DR KEGG; aei:AOY20_05660; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000064939; 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:UP000064939}.
FT DOMAIN 932..1144
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1230 AA; 143142 MW; 206ED6DEDC8B8BED CRC64;
MGIHVIQSQR IDVLLEAMLK TVQKPTTNPF EVLKPQHFIV PSPAVEAWLT QRLSEKKGIS
ANALFHHRIR GFQWAAYQWV LDEHKDKVRK ANIPRIIVKW RVFQALKEYI HEETNHLEQD
HPLYPIIQKI YDNADRLEQG IEKQLKKQSM LYWVAEQVSK LFSNYMVYRG HCQKGCEGVC
HCPSNWLDLW GNNQALDIEN MFFKTNGDIS SFVLQQAYEL EAWQRWLWQE GFHQDFQDME
EIDELFWQAL GNPENPTDAV KKLPQKLVVF TLLDLPSSQL NFLRRLGQYI DIFVLHYNPS
QEYWADSVDP KWKVRYDVRV KERFIEKNPK ATDEEIQKFF EKFTLNFNAE KRESRHPLLT
RLGKQARDHF SLLSSLSSGE EGVWADLFVN DYADTLLAKV QSDILYLVEP EAHAYTLKPN
DDSIQIHVCH SSQRQLEVLK DQLIHWLSKS TAENPRKPSD ILVLSPNLKG IESLIRSTFA
PPPSTRNLAS SYTLSAQRLS QDTVYLPIQI AGVTQLDASN AWRAVLGRIQ LIQSRFTLED
FADWLSLNAT LVRYDLDIHC VERMIALLTD AGFKRGFDEE HLKQSLSEGD EDFRFSFKFA
LDRLALGIAI PEHALFHDIL SYSQVSPGDF ELIAKLIEIY HDFNYRRDWM IAYELERNIH
VEQWLKLLMK DILEFIDAGV DALSSVFKIV KKQERMLTLA NFYDEDNHHA LGELSLPLPY
LIEEINHLID AQLEQAEPTG QITFSQIGQI RPLPYKLIVV LNLDGGKFPN RNVNLPFDLM
DILKPQLGDR SRLEDDQGAF LDVLLLAQEN LWLFYNGFDI NDGEVRDPST VLQELVQHLE
LIVETSDKSE KALSEITSVN GLSIPKHLKS LYHIHRLQPF DPLGFEEQHE VRYRDQWFKV
ANQIRSVKEQ REGWANTTYP LFDEDIQVLD SQQWINDVTF PARLYLKNLG IKNLSPSDVP
TSFEPLLLDG LGRYALRDFL HQYQESANQE LLMDRLPVGK IQESAWQMSL IEQEQLKHRL
QKYASEETVT THQVWRINAD LHMNVVLPKH SATHWVSINA SSARANRRAK VWLEYLLWLA
YLNLAEGGAD YQRIVVFSDQ TILCEGVSSN QAKQWLQLWL DAWEFGKTQP LVLPAALILK
VMEKGKELEW QSDANGNMVI QNMDDILKTW NENGQFSGFD VRSNESSKYH RDWQFILQEQ
DVQALLESAC EQFSYNLYQP IFWHQKTLED
//