ID A0A011SF53_9LACT Unreviewed; 1261 AA.
AC A0A011SF53;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=ADIAL_2068 {ECO:0000313|EMBL:EXJ22482.1};
OS Alkalibacterium sp. AK22.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alkalibacterium.
OX NCBI_TaxID=1229520 {ECO:0000313|EMBL:EXJ22482.1, ECO:0000313|Proteomes:UP000020164};
RN [1] {ECO:0000313|EMBL:EXJ22482.1, ECO:0000313|Proteomes:UP000020164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK22 {ECO:0000313|Proteomes:UP000020164};
RA Singh A., Pinnaka A.K.;
RL Submitted (JAN-2014) 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:EXJ22482.1}.
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DR EMBL; JANL01000042; EXJ22482.1; -; Genomic_DNA.
DR RefSeq; WP_034303166.1; NZ_JANL01000042.1.
DR AlphaFoldDB; A0A011SF53; -.
DR STRING; 1229520.ADIAL_2068; -.
DR PATRIC; fig|1229520.3.peg.2012; -.
DR eggNOG; COG1074; Bacteria.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000020164; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000020164}.
FT DOMAIN 11..485
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 523..817
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 1261 AA; 144674 MW; 1BF039B56AEE2C88 CRC64;
MAHIPTKPAD AQFTDPQWQA IYDGGKDILV SASAGSGKTT VLVQRVIEKI KDFTDINQLL
VVTYTNAAAR EMKERIQQAI QKEITLETDS RRKQHLIRQL PLLGHADIST LHSFCLKVIK
RYYYLIDFDP VFRLLTDDTE ISLMKEDVWE ELREELYGEE GTLFETLAAA YSNDRSDDGL
TDLIFRLYDF SRSKTDSKKW LSELSSRYAV EDEDLATSAV YQELARPDIL DILETAHELL
KDAELISNGE PELDKTLDII QADVQQVQAV KSAVLEDQLE LAYSLLNKYT FPTWKNPARK
APDEVKEAAK DMKGFRDKAK EFMQSVQSRY FLLTPKEHIA AMDEVKLLVD ELSRVSVLFF
ERYQAHKAER KALDFNDLEH LTLDILVQAD QGQLLPSEAS RHYSQQFSEV MVDEYQDINL
IQETILKWLT CSEAGTGKQF MVGDVKQSIY SFRLADPSLF IDKYERYADG KDGERIILAE
NFRSRSEVLD FTNYIFEQLM NKQVGELAYD QSAKLVNGFT AFPKAETFST EVLIYETDEE
ETDDSDDQRL EDMDVTFQMN TKTKGEIYMT ASKILELVSG DFEIYDKKLK VNRPVTFKDI
VLLTPTKKNN IEIQDIFKQL KIPTAVNDTQ NYFQTTEIAI MMALLKIIDN PKQDIPLAAV
LRSPIVGIDE VEMARIRLQD KQGSYYDALT AFIAKTNWED ERNVRLHDRL SLFMDQLNSW
RTQSKRRPLI ELIWQIYQDT GFLHYVGGMS SGRQRKANLH ALYERAASYE QSSFKGLFQF
IRFIEKMQKK DKDLAEPSAA TNGEDAVRVM TIHASKGLEF PVVFIMDMSK RFNLNNIKGS
TVLDETYGVG SEYIDTQKRI KTPTLPETVL KMQKKNRLLS EQMRVLYVAL TRAEQKLFLV
GSYKNKETAI GKWDKVSGHR ETVLPATLRL DAQSFMDWIG RCLIRHQVMA DLAGIQSANR
HVRDNQTRFS VSFHQTSELE EELLSHQTEE GDSWFEQLKE GTLKTEDDQS VSDAIRQALH
LMNAEYAYAV ATQTTSYQSV SEIKRLFEEP DDGMMVKIDV TNPRQAHRYV EDELERPSFM
SEVLQPSGAE VGKATHLVLQ AIELSEELTE AHIRSEIDRL VKEQVVSEEI AARIPVEKLD
AFFQTPFGSY ILSHVADMKR EVPFSLLLEA QDIFKDMQSV DDHILIHGII DGYIETEAGI
VLFDYKTDNV ERFGDSAADE MLKKYKGQLL IYKQALEAIL KRPVIQTQLI MLDTGETVEV
S
//
