ID A0A2C6C6Y1_9GAMM Unreviewed; 1128 AA.
AC A0A2C6C6Y1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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 ECO:0000313|EMBL:PHI32100.1};
GN ORFNames=CRN84_23660 {ECO:0000313|EMBL:PHI32100.1}, NCTC12282_06480
GN {ECO:0000313|EMBL:VFS53414.1};
OS Budvicia aquatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Budvicia.
OX NCBI_TaxID=82979 {ECO:0000313|EMBL:PHI32100.1, ECO:0000313|Proteomes:UP000224974};
RN [1] {ECO:0000313|EMBL:PHI32100.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FDAARGOS_387 {ECO:0000313|EMBL:PHI32100.1};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.J.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000224974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_387 {ECO:0000313|Proteomes:UP000224974};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:VFS53414.1, ECO:0000313|Proteomes:UP000373449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12282 {ECO:0000313|EMBL:VFS53414.1,
RC ECO:0000313|Proteomes:UP000373449};
RG Pathogen Informatics;
RL Submitted (MAR-2019) 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; PDDX01000001; PHI32100.1; -; Genomic_DNA.
DR EMBL; CAADJA010000002; VFS53414.1; -; Genomic_DNA.
DR RefSeq; WP_029094394.1; NZ_PDDX01000001.1.
DR AlphaFoldDB; A0A2C6C6Y1; -.
DR STRING; 1111728.GCA_000427805_01300; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000224974; Unassembled WGS sequence.
DR Proteomes; UP000373449; 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:UP000224974}.
FT DOMAIN 832..1050
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1128 AA; 129809 MW; A36A969FFCE1CD39 CRC64;
MFTVYHSNQL DLLKTLTTAL IAGKPLSDPF AREIILVQSH GMAQWLQIEL ANELGIAANI
EFPLPASFIW QMFTKVLPGI PQESAFSKDA MTWKLMWLLP PMLEQPEFSA LKGYLSDDED
MRKRHQLAGR IADLFDQYLV YRPEWLQRWQ QNELVNDLDD AQIWQAPLWR ALIDYTERLQ
QPGWHRANLY QRFIDTLNQP DFSAEVLPHR VFICGISALP PVYLQALQAL GQHIDVHLMF
TNPCRYYWAD IQDYAFLAKL QARKRKHIKK GQDIGLFRSP ETASSLFDEQ GNQQLNNPLL
ASWGKLGRDN LYLLAQLDKM QEVDAFVDIE SDSLLHRIQS DILSLDDRAL IINSPDSPLD
SCDKRILDPD DRSISTHVCH SAQREVEVLY DQLLAMLDND PTLTLRDIIV MVADIDNYTP
YIEAVFGNAP ADRYLPYAIS DRSASQAHPV LTAFLSLLDL PDSRFTAEDI LTLLEVPALA
MRFQIDEDGL RILRQWVEDS GIRWGLDDDM VSDLELPPTG QHTWQFGLTR MLLGYAMDSQ
RGDYQGVLPY DESSGLIASL AGQLAEFLMQ LAIWRNKLKQ SRTLTEWSPF CRELVDSFFI
TDVETEPVLA LIEQQWQKQI GFGLEARYQD LIPLTILRDE LSARLDNERI SQRFLAGPIN
FCTLMPMRSI PFKVVCLLGM NDGVYPRTLP PLGFDLMARK PLRGDRSRRD DDRYLFLEAL
ISAQQKLYIS FIGQSIQDNS PRYPSVLISE LLEYISQSHR LPDDRHLDLE QSALKVYQHL
LCQHARVPFS EQNFVSGSEQ QSYASEWLPA AGRAGIPHAE FSTDLDELEL KRVELEDLRR
FYRNPVRAFF QQRLRVNFSL DETELPDEEP FLVDNLQRYQ MNVMLLNSLI EDQDPAALFS
RARAAGELPF GAFGELFWQG QSEDMAELAE VVKQHKLPAQ SIEFEHNIAG LEITGWLHQV
QADGILRWRP AELSVIDGML LWLDHLVYCI NGGSGESRMF GRKNSEWRFA AMPTEQAEEI
FAEWLNGYVH GLSTPLLLLP KSAWAWLTNC YDQSSGRILW DEEIQQKARQ KLIQVWQGGQ
QVTGEGEDPY LMRLFRVMDD KRYQQIISDS QPYLFTLIRH KLENQKSG
//
