ID   ADDB_ALKOO              Reviewed;        1144 AA.
AC   A8MJ51;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000255|HAMAP-Rule:MF_01452};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01452};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01452};
DE   AltName: Full=ATP-dependent helicase/nuclease AddB {ECO:0000255|HAMAP-Rule:MF_01452};
GN   Name=addB {ECO:0000255|HAMAP-Rule:MF_01452}; OrderedLocusNames=Clos_2300;
OS   Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS   OhILAs)).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=350688;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OhILAs;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA   Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT   "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL   Submitted (OCT-2007) 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 AddB nuclease domain is not
CC       required for chi fragment generation; this subunit has 5' -> 3'
CC       nuclease activity. {ECO:0000255|HAMAP-Rule:MF_01452}.
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_01452};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01452};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC   -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000255|HAMAP-
CC       Rule:MF_01452}.
CC   -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01452}.
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; CP000853; ABW19833.1; -; Genomic_DNA.
DR   RefSeq; WP_012160140.1; NC_009922.1.
DR   AlphaFoldDB; A8MJ51; -.
DR   SMR; A8MJ51; -.
DR   STRING; 350688.Clos_2300; -.
DR   EnsemblBacteria; ABW19833; ABW19833; Clos_2300.
DR   KEGG; aoe:Clos_2300; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
DR   Proteomes; UP000000269; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008409; F:5'-3' 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-EC.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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_01452; AddB_type1; 1.
DR   InterPro; IPR014140; DNA_helicase_suAddB.
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   PANTHER; PTHR11070; PTHR11070; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR02773; addB_Gpos; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; DNA damage; DNA repair; Exonuclease; Hydrolase; Iron;
KW   Iron-sulfur; Metal-binding; Nuclease; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..1144
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379149"
FT   DOMAIN          1..276
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   DOMAIN          274..584
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         784
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1102
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1105
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1111
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ   SEQUENCE   1144 AA;  133797 MW;  6638D538F3692E06 CRC64;
     MAIRYVFGRA GRGKSYFVLE EIKKRLEGEG HHKLFLLVPE QFTLQAERDL IGKQALKGIM
     RAEVLSFTRL THYVFNEVGG ITKIPINEIG KNMILRKIAD ESSKDLSIYK SIAKQEGFIT
     KLNDLICEMK QHDITPIELT MEFNEMEEDT LLKRKLNDII LLYQKFNNYL RDRYVDNEDN
     VNLLIENIEK VQFLEGAEVW IDGFQSFTPQ IFRVIEKLAE KVKNLTITFT MELKSKESDQ
     DLFHINRKTY LKIKSIAQRL GLEEEIIDLD RNERPVLPKV QEICHIEKEL YAYPYQQYTG
     EITHLDVFSG SNLYTEMENV AAQIIHLVRD KGYRWKDIAL VSAGLEEYSM ILKRVFEEYS
     IPYFMDEKRS IMNNPIVELI LSSIGILARG YQYEDVFRFL KTGFGDLNKD EVEELENYVL
     QYGIKGKDYA VPFTKGFTNK KHEEIEQEES DEIHEEKIKY NEFRERFIAP FLKFEKKIYR
     KKKVGHITKA LFEFMKDLNI EAKLDQWIEE LREKKYFEYV NENTQIWNKV MEILDQLTEI
     LAEESTTLKE YGRILEAGFL ACEVGVIPTT IDQVLVGSIE RSKSHDIKAL FVIGVNDGIL
     PSSREDGGIL LDHERESLDK KGLSIGNTLE NALLEEQFTI YSALSKPTEY LWISYALADQ
     EGKAQRQSIL IDRIKKLFRN LNIQSDVVPT LNRQLHLITT PISTFKYMTE SIRQNIDDKP
     MEDIWWDVYQ WYSNESQWDE RRNLMVKGLF HENQISYIGE QKARSLYEHP IKSSVSRLER
     FANCPFSHFV TYGLRPKERK EYQLSNPDIG RLFHDSMENF TKELVNEQIQ WKDLTREQSD
     YFVEKVIDEM VPEFEHGIML STHRYQYLVT RLKRISKRAM WTLTEHIKKG QFVPMGHEII
     FGLEGDIPPI VIELESGEKI YLEGRIDRVD ILNDEDGNYV KIIDYKSGSK EFSLSDVYYG
     FQIQLLVYLD AVLSSQSQKY QAEVHPGGIF YFKIDDPMVK TTEKAVKEVE KEINKRLKMK
     GLVLKDVNII KKIDEDIGRS SSILPASLTK EGEISKTSSA LPEEDFKALL KHVRGLVKEI
     GEEMLKGNVK IEPFKKGGDT SCKYCAYISI CQFDHSFHEN QYKTIKELKN EEVLEKIRKE
     NENI