ADDA_LACGA
ID ADDA_LACGA Reviewed; 1204 AA.
AC Q043G6;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000255|HAMAP-Rule:MF_01451};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01451};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000255|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; OrderedLocusNames=LGAS_1031;
OS Lactobacillus gasseri (strain ATCC 33323 / DSM 20243 / BCRC 14619 / CIP
OS 102991 / JCM 1131 / KCTC 3163 / NCIMB 11718 / NCTC 13722 / AM63).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=324831;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33323 / DSM 20243 / BCRC 14619 / CIP 102991 / JCM 1131 / KCTC
RC 3163 / NCIMB 11718 / NCTC 13722 / AM63;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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:0000255|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=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
CC -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000255|HAMAP-
CC Rule:MF_01451}.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01451}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000413; ABJ60406.1; -; Genomic_DNA.
DR RefSeq; WP_003652957.1; NZ_WBMG01000008.1.
DR AlphaFoldDB; Q043G6; -.
DR SMR; Q043G6; -.
DR GeneID; 66469047; -.
DR KEGG; lga:LGAS_1031; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR BioCyc; LGAS324831:G1G6Y-1031-MON; -.
DR Proteomes; UP000000664; Chromosome.
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:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 4.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR014152; DNA_helicase_suAddA.
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 PANTHER; PTHR11070; PTHR11070; 1.
DR PANTHER; PTHR11070:SF48; PTHR11070:SF48; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR02785; addA_Gpos; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Nuclease; Nucleotide-binding.
FT CHAIN 1..1204
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379282"
FT DOMAIN 2..469
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 497..784
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 23..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1204 AA; 139135 MW; 414B921B5C2C4DA8 CRC64;
MTNFTKEQDQ AINDAGKDIL VSASAGSGKT TVLVERVLKK ILSGTPVSSL LIITFTKAAA
REMKERIKQK ISDQLEIEPD NQFLRSQLLD VDTANISTID SFCLDVIRRF YYVIDLDPQF
SVLTDETQAE LLKERALREI EADYLEGDNQ DFQDFYDNFS GDRDAEGARN LLLQLYNTAT
TEPNYEKFLD NLPTCYEVGD NLIRSNLWQQ QIKPLLLKEI SDLKAEVEAL LAEPEINSSD
LVKVKENYDI FSNRLDSFWE SLNTDQPYNE IRANLMNCKF EKAVRKSKKW SDESIEVYQD
SQDLKLDLND QLKKIFASFF VVEEKEQIAV LQKSEKIVKT IVAAEKKLIQ KFSQLKREQN
LIDYSDMEQF AFSILTTDTS NAHIAQEYYQ EKFNEILIDE YQDVNALQEN IIKAIKKKGQ
NTLFMVGDVK QSIYGFRQAR PDLFLSKYHT YGKDNDSEKI ILADNFRSTK RVTKTVNDLF
NPILTTNFGG IDYKKEGQLQ FGASYYPSDL PTASEYIFTD KKQTQSAYED QYGDEMDFSE
VQMVIARIKQ LKAENFQVWD RRTQLKRPLE YSDIAIITRT RSDNLQVMQE FAKADLPLFV
TDAQNYFQTF ELIMIMNYLR LIDNPQQDIP LVAVMRSPLF NFKEPELAQI RVKTPAGNFY
TALTSFASVN SSLGKKCKEF LQQLETLRSF AATHRISELI WSIYEKTHLL EIVTGLPNGQ
QRRVNLESLY ERATSYESAG FKGLYQFISF IERMRKNQKD LAQPLLSDKA DNAVKLMTIH
ASKGLEFPIV FVMGLGHQYQ TRDLSGNFTI SQNELGLTIK EKNYRIDSLV KSLADVQKRQ
QMLEEEARIL YVGLTRAQQK LILVASVNEI ENKRKKWVSE LDQKKDIIPL VKKINAQSPL
DFLGPKLEQK HEFDQTIRDM TSALEEQDKL YYLKFNLDLE PEKIKDQNED SQEVNSNVNK
VVKELYNFKY PFEDATKTTA YQSVSEIKKA FNDPIDTELE NSRLISSSNR YLQPIDETPT
FLEGQKFTGA EIGTAMHLVL QYYNYEGNKD QENLDQEIDQ LVELGKLNSL MVPHLSKEAL
NWFVMSDFAK EFWKQPDKLH RESQFSSLVN ASELFNDFSD PSAKVLVHGT VDGYFEAKDG
LILFDYKTDF VDKTNEEQAI EKIKQKYTGQ LRLYEQALNE MNNDKKVIGK YLILLDARKV
VPVD
