ID A0A0Q3SX34_BRECH Unreviewed; 1278 AA.
AC A0A0Q3SX34;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=AN963_15020 {ECO:0000313|EMBL:KQL46278.1};
OS Brevibacillus choshinensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=54911 {ECO:0000313|EMBL:KQL46278.1, ECO:0000313|Proteomes:UP000051063};
RN [1] {ECO:0000313|EMBL:KQL46278.1, ECO:0000313|Proteomes:UP000051063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8552 {ECO:0000313|EMBL:KQL46278.1,
RC ECO:0000313|Proteomes:UP000051063};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (SEP-2015) 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:KQL46278.1}.
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DR EMBL; LJJB01000010; KQL46278.1; -; Genomic_DNA.
DR RefSeq; WP_055745359.1; NZ_LJJB01000010.1.
DR AlphaFoldDB; A0A0Q3SX34; -.
DR STRING; 54911.AN963_15020; -.
DR PATRIC; fig|54911.3.peg.1003; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000051063; 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 CDD; cd18807; SF1_C_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|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}.
FT DOMAIN 12..493
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 534..840
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1278 AA; 144423 MW; 98F7B49568EF1A1A CRC64;
MTTQQLTQAK PEQWTDEQWQ AITQRGNNLL VAAAAGSGKT SVLVERIIRR IMDETEPIGV
DQLLVVTFTN AAAAEMRHRI GDALRKALKE DPHSAHLRRQ LALLQRATIT TLHSFCLGIL
RQYYYLIDLD PDFRIADQME GELLRQDVLE EQLEGWYEDD VDFHALADVM LDGQDDQILA
TLLLRLYEFS RSHPEPSHWL QDAADMFAAA GRNGLDGLKW AKSVLRSLEL ELAAMEGKMR
RAVSLASSPE GPAAYLPLLE AEADALKRAS YACRMGWEAT QQAVNLVSFA KLPPVKGTDT
EIKEQVQDLR NSVKKSLGEL NEQYFSMSAD QYVADLHAIA PHMNTLSRLV TAFAAAFQQE
KRSRSIVDFG DLEHLALRVL TEKREDGTTV PSQVSLQLRE QFAEVLVDEY QDINLVQETL
LQMVSRDAVI NGTANRFMVG DVKQSIYRFR LAEPKLFLEK YLTYQKDGES IESARDTEPT
GLRIDLAANF RSRREVVDSV NYLFRQIMSP GVGEIDYDPS AELINRASYP EVEEGRLQAE
VHLIDRKSSQ ADGEVLPVSE GTEEAETASI PDGTVENAEE VSVAQLEARL IASRIRRWME
PGEGEAPLLV FDKKAGGLRP LAYRDIVILL RATSGWGETM QEELREAGIP VYAEQTAGYF
AATEVETMLS LLRVIDNPLQ DIPLAAVLRS PIVGLREENL AQIRIRYTSG PFYQAVVQYA
EEQQAEEGWE KRLRYFFSRL RDWRTHARRG ALSELLSVLY RETGYLDYVA ALENGQQRQA
NLRALYDRAR QYEAGSYRGL FRFLRFVDRL QEAGNDLGEA RTIGENEDVV RIMTIHKSKG
LEFPVVFVAG MGKQFNTMDL KSQFLLHKDL GFGPMAFEPT LQLRYPSLAA LGIRQQLRRD
MLAEEMRVLY VALTRAREKL IMVGSAKDLA KSVTDWGRQG DQERLSDEDL IQAKGYLDWV
GRALLRHPAA GLLRAYPQER GTGETVSVRS IPDDSEWSFH FYQADELREQ AAATADAAAV
WERMSRREEI IERPEDAGQR EKIESTLGWS DPHPVAPHVP AKWSVSELKR QARTGKSGAP
IVLPSITEKP KFLTEQKPSR LSGAEKGTIT HLLMQHLDLH RPLDEADIRE QLADLAARRF
LTEEQLGAVD VGQIVRFFAD PLGSKMKQAK VVHRELPFTM TIPAHEVEPE LEEESNEQVI
VQGVIDCLLE EQDGRLVLID FKTDWMAKEP SPAVIEEITK RYEGQIKLYV QAIQQITKTE
REIDSYLYLL AGGFAVRV
//
