ID H8L504_FRAAD Unreviewed; 1143 AA.
AC H8L504;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
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 OrderedLocusNames=Fraau_1276 {ECO:0000313|EMBL:AFC85718.1};
OS Frateuria aurantia (strain ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 /
OS NBRC 3245 / NCIMB 13370) (Acetobacter aurantius).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Frateuria.
OX NCBI_TaxID=767434 {ECO:0000313|EMBL:AFC85718.1, ECO:0000313|Proteomes:UP000005234};
RN [1] {ECO:0000313|Proteomes:UP000005234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 / NBRC 3245 /
RC NCIMB 13370 {ECO:0000313|Proteomes:UP000005234};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Frateuria aurantia DSM 6220.";
RL Submitted (FEB-2012) 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; CP003350; AFC85718.1; -; Genomic_DNA.
DR RefSeq; WP_014402724.1; NC_017033.1.
DR AlphaFoldDB; H8L504; -.
DR STRING; 767434.Fraau_1276; -.
DR KEGG; fau:Fraau_1276; -.
DR eggNOG; COG1330; Bacteria.
DR HOGENOM; CLU_007513_1_0_6; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000005234; 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; 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:UP000005234}.
FT DOMAIN 829..1070
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1143 AA; 128794 MW; B8BE4CDBBF17BBFC CRC64;
MTTAAALTPG LMVIHGNQIE DLRELCVAWM RRHPLRPLEN ERFLVYSNGI AQWLKQALAE
DAGCGIAAAL QFDLPSRFMW SAYRLVLGEA AIPTQSPLDK APLTWRLLRL LPECLHQEVF
APLRHFLADD PDLRKRHQLA ERLADLFDQY QVYRADWLND WAAGRDELRS LRHGAIPLQP
QQLWQPALWR ALLADINDPE LVQGRAFVHP RFVAALETME QPPVGLPRRI IVFGITSLPA
QALEALAAMA RFSQVILCVH NPCQHHWGDI VEDKDLLRHQ YRRHPHRPGQ IIGAELLHAQ
AQPLLAAWGK QGRDYINLLD RHDDPERYRE HFERIDVFEP PASDHLLGQL QDDIFDLRPL
RESRELWPAV DPARDHSIRF HVAHSAQREV EILHDQLLAA FSADPALRPR DIIVMVPDIQ
TYAPAIQAVF GQYPRGDARH IPFTIADQGV RGQSPLTIAL EQLLQLPRGR LAVSDVLDLL
DAAPLRQRFG IAEQDLPQLR QWLDGAGIRW GLDAGQRAAL GQRAGLEQNT WDFGLRRLLL
GYASAEEAFA GIEPYADIGG LDAALLGPLI DLLQALRQPL QQLAEAHAPA AWGMIFRQLL
EQFLRPVDEQ DQALVDQLLK ALDDWLDLCR DAGLEDALPL SVAREGWLAT LDQGGLSQRF
LSGAVNFCTL LPMRTIPFRQ VCLLGMNDGD YPRSKTPMDF DLMAGDYRPG DRSRRDDDRY
LLLEALLSAR DRLHVSWVGR SIRDDSERPA SVLVGQLRDH LVSGWRLAGG GDLLQALTTI
HPLQAFSRRY FEADTAWYTH AGEWAAVHQT PTEDARSAPS LPAWQDPPPL SLDRLQAFLA
DPVRAFFQQR LGIHLDQYGE ELQDDEHFGL DGLQRYSLTQ ALLDETRQQL DLQGAELAPA
LALAAQRLQG RGQLPLAGFG AALRDELLDP LPDQFQRYRQ QRERWSRPLA ATLPLQFVHG
TLRLDDWLGG LCRDADDQPA SLQLLPRRLL NKKALNWHRL LKAFVTHAAA CASGIGLHTV
LIAEDVSVSW APLPQPTAET ILADWLDGWA QGMCQPLPTA RKTALSWLAH AEEDLSRAWK
EAARTYQDDF THGGEVRHSA SLARQYPDFA QLVAEPEAFA RWAKQLYRPL LQHPPTLLDA
DSP
//
