ID A0A495RHB9_9GAMM Unreviewed; 1107 AA.
AC A0A495RHB9;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
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=DES39_0019 {ECO:0000313|EMBL:RKS86821.1};
OS Orbus hercynius.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Orbales; Orbaceae; Orbus.
OX NCBI_TaxID=593135 {ECO:0000313|EMBL:RKS86821.1, ECO:0000313|Proteomes:UP000278542};
RN [1] {ECO:0000313|EMBL:RKS86821.1, ECO:0000313|Proteomes:UP000278542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22228 {ECO:0000313|EMBL:RKS86821.1,
RC ECO:0000313|Proteomes:UP000278542};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (OCT-2018) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKS86821.1}.
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DR EMBL; RBWY01000001; RKS86821.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495RHB9; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000278542; Unassembled WGS sequence.
DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:RKS86821.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01486};
KW Membrane {ECO:0000256|SAM:Phobius};
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:UP000278542};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 214..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 803..1030
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1107 AA; 128912 MW; 1CEEB05C50B174A1 CRC64;
MLTIYHSNQL DLLKSLTAQL IKRQPLNAVF EKEVILVQSQ GMGQWLQIQL AQELGIAANI
HYPFPTQFVW DIYRIFYPEL PQKNAFDADF MLWVLLAILP DLAKTPSFSA LQRYFEQENQ
QKYYQLASCL ADLFDQYLVY RPDWIKAWEA GELVAELSQD EQQWQAILWR EMIAYSQRLS
SKPLHRADIH HTVIAALKQK KLTRTQKKSL PKRIFIFGIV SLPPLYLALF NALSLHLDVH
IMFMNPCRQY WGDIVDRSFV NKYIDDEHVA NMMLQQSHPL LASWGKLGRE HLVLLQDFQK
QDIDAFFDYD ERTLLASVQQ SILDLHSEPE LAANSYLLSS SEHKQEILRN DDSLTIHACH
SEQREVEVLY DYLLATLDRH QSIDLNDCVV MVADIEHYAP YIQAVFDNAP KNRYLPYTIS
DQTFRYIEPI VQGFFLLLEL PKSRLEIEYI FDLLEIPPIA RHFNLNAENL VQLRHWIVDA
GIRFGLDSNT DEPHSWLVGI QRMLLGYIME SQLDSWQDIF PYDGTTGLDA ELVGFLADFI
AAIAKWHRLL SEPHSITQWQ SLCAPLLDEF FLFDSDSEAL LMMIEEQWQN IIEQALAANY
CDELSITVLR ELLQSKFQHN AISHRFLIGK INFCTMMPMR SVPFKVVCLL GMNDGVYPRG
ISPLGFDLIY HHSRIGDRSR RNDDRYLFLE ALLSAQQQLY ISYIGYDIQT NELRYPSILV
DELIEYLKQC YVLNGDQHLD GESSAAGLVN HLIHVHTRMP FSRQNYLPGD TKIVSYADEW
LAAAKDAGQF SNFITPLSQE LIEDINLDKL KQFYLHPIRE LAKYRFGYVI NYIDEQLPST
ENFNLNNLER YHLNNQILDV LLSNNLTGEQ LADKLYQKML HSNQLPYGAF GQILYREQQK
LIEPLISRIN KEKQESCSSL DVDIMVDDLR IIGRIQRIQC DGILQWRSTK LTVKDGIVLW
IEHLVMCILQ PDSHLLRNRI YGREETTWCF RTLLSQQAQV LLSQLLGAYL TGLNQPMFMP
LQSTWRWLET AYDATTQHIS KDSAVLLKAK TQFITQWQGH LAIRGECDDY YIRLYPELTD
ELINEAIQNA MIYLLPLMVY REIDDAD
//
