ID A0A151ALB4_9CLOT Unreviewed; 1240 AA.
AC A0A151ALB4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000256|HAMAP-Rule:MF_01451};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01451};
DE EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000256|HAMAP-Rule:MF_01451};
DE AltName: Full=DNA 3'-5' helicase AddA {ECO:0000256|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000256|HAMAP-Rule:MF_01451,
GN ECO:0000313|EMBL:KYH28415.1};
GN ORFNames=CLCOL_19070 {ECO:0000313|EMBL:KYH28415.1};
OS Clostridium colicanis DSM 13634.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121305 {ECO:0000313|EMBL:KYH28415.1, ECO:0000313|Proteomes:UP000075374};
RN [1] {ECO:0000313|EMBL:KYH28415.1, ECO:0000313|Proteomes:UP000075374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13634 {ECO:0000313|EMBL:KYH28415.1,
RC ECO:0000313|Proteomes:UP000075374};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium colicanis DSM 13634.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA helicase
CC and an ATP-dependent, dual-direction single-stranded exonuclease.
CC Recognizes the chi site generating a DNA molecule suitable for the
CC initiation of homologous recombination. The AddA nuclease domain is
CC required for chi fragment generation; this subunit has the helicase and
CC 3' -> 5' nuclease activities. {ECO:0000256|HAMAP-Rule:MF_01451}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618, ECO:0000256|HAMAP-
CC Rule:MF_01451};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01451};
CC -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000256|HAMAP-
CC Rule:MF_01451}.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01451}.
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:KYH28415.1}.
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DR EMBL; LTBB01000010; KYH28415.1; -; Genomic_DNA.
DR RefSeq; WP_061858732.1; NZ_LTBB01000010.1.
DR AlphaFoldDB; A0A151ALB4; -.
DR STRING; 1121305.CLCOL_19070; -.
DR PATRIC; fig|1121305.3.peg.1911; -.
DR Proteomes; UP000075374; Unassembled WGS sequence.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR014152; AddA.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; TIGR02785; addA_Gpos; 1.
DR PANTHER; PTHR11070:SF48; ATP-DEPENDENT HELICASE_NUCLEASE SUBUNIT A; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01451};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01451};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01451};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01451};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01451}; Reference proteome {ECO:0000313|Proteomes:UP000075374}.
FT DOMAIN 4..473
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 514..809
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1240 AA; 144666 MW; 002A7A8823C682F6 CRC64;
MEDTKWTKEQ QDAIDTHDCN LLVAAAAGSG KTAVLVERII KMITDFKNPI DIDRLLVVTF
TNAAASEMKE RIAKAISDEL TKHPKSRQLQ RQLTLINRAS ITTMHSFCLE VIRNNFHYID
LDPNFRIGDE TETILLKGEV IEEMFEEMYE SEKCSPEFLS LVEFYSSNKN DLELQNIVLN
LYNFVMASPN PRDTLIKMAE DFNVDEDYDF GKSKWAKVLM EGVKIEAIGL KKKMENAIKI
INETEGLEPY LENFQSELNM IKEVIVSTDI SWSSLFDSLE GVKFGKLKPC KKCQDKDAQD
KVKKIREKVK KRLQNDIKMR IISYSSKETA LDLKSLYPVM KALSNLVLEF MDRYAKAKRD
RGIIDFNDFE HFCIDILKHP EVSSRLREKY VEILVDEYQD SNDVQEAIID FIARKDEATG
KNINVFMVGD VKQSIYRFRQ AKPELFLQKY NTYSTEEGAA ERKIKLFKNF RSRKEILDGT
NFIFKHIMSE SVGELEYDED EALNLGADYE EYEGDKSLVA GPIEINIIEK NYEDLGSDDT
EEKEEELLDN IQMEARFVAK RINELVNPKY GEPFKVYDRD LKAYRNIEYK DIVILLRSTS
KWAPVFMDEL KENLVPAYAD VGSGYFESLE IKTILSLLQI IDNPRQDIPL IAVLRSPVAS
FTPEQLIDVR MASKTGDFYE GILNIANNEY NDGIQNELKE KCSVFLEKLK IWRDKSIHMP
IDEFIWYLYT DTGYYGYVGA LNGGIQRQAN LRILFERARQ YEKTSYKGLF NFINFINRLK
VSSGDMGSAK ILGENDNVVR IMSIHKSKGL EFPVVFLSAL GKNFNMKDLN RRILFHGELG
FGPDYIDLEK RLSYSTVVKE ALKDKIKIET LSEEMRILYV ALTRAKEKLI MTGAVNDIEK
HCKEWSYGLY DDDQKLSQHE ILKAKNYLDW ICPVVMRHKD GEPLRNKSGI QEYEKITLIE
DDSKWNVEFY NISSVINEKK EDIGQIELES IEDIENIRLN SIYYDEINER LNWKYSYMEA
SKLPTLLTVT ELKRMQNRDM YDDYSTNIYT PSLVKRPSFM EKDRKLTGAE KGTAIHAVMQ
KIDYKRELNR EEIEKQIKEL VENELITEEQ AKSVDISKIL NFFNSNIGKR MIKSEKVYRE
VPFHMEIKST EVYRDLPKDK YMNENIMVQG IIDCYFEENG KVILIDYKSD YFKKGEEKAI
IDKYKIQIEF YARAIEKITN KKVKEKYLYL FYGDKEVEVK
//
