ID A0A143YA43_9LACT Unreviewed; 1269 AA.
AC A0A143YA43;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 ORFNames=Tpal_666 {ECO:0000313|EMBL:CZQ85676.1};
OS Trichococcus palustris.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Trichococcus.
OX NCBI_TaxID=140314 {ECO:0000313|EMBL:CZQ85676.1, ECO:0000313|Proteomes:UP000242754};
RN [1] {ECO:0000313|EMBL:CZQ85676.1, ECO:0000313|Proteomes:UP000242754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Trichococcus palustris {ECO:0000313|EMBL:CZQ85676.1};
RA Wen L., He K., Yang H.;
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}.
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DR EMBL; FJNE01000002; CZQ85676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143YA43; -.
DR STRING; 140314.SAMN04488076_101149; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000242754; 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 Gene3D; 1.10.274.50; -; 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; 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; 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|ARBA:ARBA00023235, 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:UP000242754}.
FT DOMAIN 11..486
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 513..822
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1269 AA; 146613 MW; 5DC0C5506627400A CRC64;
MTGIPARTPN EKFTETQWQS IYQTGDNILV SASAGSGKTT VLIQRIIEKV KGGTNVDELL
VVTFTESAAK EMKERMTSAI QSAINQAETQ EQYLHLIKQL SLMPQANIST IHAFCLKVIQ
RYFYLIDLDP VFRLLADTIE VELLKEDVWE EVKEELYGEP DTFFKKLAKA YSKDRSDEDL
MKLVFSLYEF SRANPNPYRW LDSLPMLYNT DEGLVNSLLY RELLKPQMLS LIEGIRYDAE
QALHLAGEDS ETAPQRELLE TECGYAVQLL EAIQQDDYEK GYRIVTEQLN FARWTGSKKA
DDDELKERKG QLKDLRDKYK EDFGALTKQY FNRPLAEQEQ VLQGIRPYAE EMARVTKRFS
EAYWERKLAD NVLDFNDLEH LTLQILAPFA PNGERQMSDA SAYYRNKFQE VLIDEYQDVN
QLQESILYWV TRHQPETENL FMVGDVKQSI YAFRLADPSL FLRKYAAFAD KNGGERIILA
ENFRSRTEVI GFTNFIFEQL MDERVGQMAY DEAAKLQAGN KSFPESERNQ TELLIYLSEN
ADSDEEVLTE ENDLEADMTI DDKTAGEVTM VAQKIRALID EHFPIYDKKT KSERPLSYRD
IVLLTPTKKN NLVILEIFKD FQIPVILNDT ESYFQRTEVS IILSLLKVID NPRQDIPLAA
VLRSPIVGLD EKQLALIRIH HKNGDFYDAV QHFMMLYNTG AIGHTAEFKD IHTRLERFLA
QLAEWRNLSR RSSLVTLIWT IYNDTHFLDY VGGMVAGKQR TANLHALYER AKKYEETNYK
GLFQFIRFIE KIQQRDKDLA EPTSFSDDED AVRVMTIHAS KGLEFPVVFL MDLSKRFNLS
DTRSSYIFSE KYGLGTDYFD VDQRVQYPSL ARQALAIEKK KNLLAEEMRK LYVALTRAEQ
KLFLVGSYKT EEKLWADWHV ADGTRGKMLP DYLRLQASSM MKWLGMCLYR HEDAENDYFH
REYKGELTHY PVHFAVSTFR EEDLLSFIPV ALEEINESEW KDEIEKMANG KVEPHDHSLA
EDMRLAVALM EAKYPHQAAT TTTSYQSVSE IKRLFEDPDE THMLKLDLAD TKRVSRYVEP
DFPHPKFMQE TVTPTSAEIG TATHFVMQSV DLTQDITETY VAQLLLELVG DGLLQEAVAA
KINVEQIALF FQTALGQEIQ VNADKVRREM PFSLLIPAGR IFAEISEEDG DNLLIHGIID
GFIEYEDNIV LYDFKTDFVS DRPPFLPENI VEKYKGQMNL YKKGLETIRH KPVSAVYICL
LSNNTNISI
//
