ID A0A427KDE7_9GAMM Unreviewed; 1122 AA.
AC A0A427KDE7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=EGK14_02055 {ECO:0000313|EMBL:RRZ97099.1};
OS Erwinia sp. 198.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=2022746 {ECO:0000313|EMBL:RRZ97099.1, ECO:0000313|Proteomes:UP000273595};
RN [1] {ECO:0000313|EMBL:RRZ97099.1, ECO:0000313|Proteomes:UP000273595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=198 {ECO:0000313|EMBL:RRZ97099.1,
RC ECO:0000313|Proteomes:UP000273595};
RA D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT "Transmission dynamics of multidrug resistant bacteria on intensive care
RT unit surfaces.";
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:RRZ97099.1}.
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DR EMBL; RHUM01000001; RRZ97099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427KDE7; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000273595; Unassembled WGS sequence.
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}; 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:UP000273595}.
FT DOMAIN 829..1048
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1122 AA; 127913 MW; BDB8B68953BAEA0C CRC64;
MFTVYHSNQL DLLKTLAAFH IENQPLRDPF QSEVVLVQSP GMAQWLQMSL AEQFGIAANI
AFPLPASFIW DMFVRVLPGI PKESAFSKAS MSWKLMTILP KLLARPEFVM LSHYLSDDED
KRKLFQLASR VADLYDQYLV YRSEWLNSWE KGQQIEGLGE AQQWQAPLWA ELVAWNRELG
HPEWHRANLY ARFIATLEQS STRPPNLPDR VFICGISALP PVYLQALQAL GKHIDIHLLF
TNPCRHYWGD IQDYAFLAKL QSRRREHYKQ QRESALFREE DAASLFNDAG EQQLSNPLLA
SWGKLGRDNL FLLAQMECRE IDAFVDIEPT TLLQTLQRDL LELEDNAVIG LKREEWESSL
GKRVLDPDDQ SVTFHLCHSP QREVEVLQDR LLAIMAEDPQ LSPRDIIVMV ADIDAYTPFI
QAVFGNAPAE RWLPFSISDR RASQAHPALQ AFISLLSLPD SRFTSESVLA LLEVPAVASR
FSIDEEGLRR LRHWVGECGI RWGLDDDTVR ELDLPPTGQH TWQFGLTRML LGYAMHSDIG
HWQGVLPYDE SSGLIAELVG HLAELLMQLR RWRERLSEPR ALEAWLPLCR ELLGDFFAGD
AEAEAALALI EEQWQQAISY GIQAEYQQAI PLSLLRDELR ARLDQERISQ RFLAGPVNFC
TLMPMRSIPF KVVCLLGMND GVYPRTLPPP GFDLMSQQPK KGDRSRRDDD RYLFLEAINS
AQHQLYISYI GRTIQDNSER FPSVLVSELV DYIGQSFCLP EDRQSDVDTS AARVIAHLHH
LHSRMPFAAE NFLPQARYQS YAAEWLPAAK ASGVPHPPFM QPLPEENITE LNFDQLLRFW
RHPVRAFFSL RLGVSFSAED MELPDAEPFI LDNLSRYQLN TQLLNTLIEG QPGEPLFDRH
RAAGNLPYGA WGELFWQDQL ADMAELAGVV REQRKDAVSQ EINLQVGGLQ LSGWLPAVQD
DGLLRWRPGH LNFTDGLALW LEHLVYCVLG GSGASRMYGR KESRWWFPPL SAVEASGWLE
RYIEGYKAGM CAPLLLLPKT GGAWLEACYD EKAAAVSYDE ATQAKARNKL LQAWQGNIQT
EGEGSDPYLA RLFRTLDEAT LQQITHNAEV WLLPLLRMND IN
//
