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Database: UniProt
Entry: A0A2M8TFL3_9CLOT
LinkDB: A0A2M8TFL3_9CLOT
Original site: A0A2M8TFL3_9CLOT 
ID   A0A2M8TFL3_9CLOT        Unreviewed;      1153 AA.
AC   A0A2M8TFL3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000256|HAMAP-Rule:MF_01452};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01452};
DE            EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01452};
DE   AltName: Full=ATP-dependent helicase/nuclease AddB {ECO:0000256|HAMAP-Rule:MF_01452};
DE   AltName: Full=DNA 3'-5' helicase AddB {ECO:0000256|HAMAP-Rule:MF_01452};
GN   Name=addB {ECO:0000256|HAMAP-Rule:MF_01452,
GN   ECO:0000313|EMBL:PJI09771.1};
GN   ORFNames=CUB90_18700 {ECO:0000313|EMBL:PJI09771.1};
OS   Clostridium sp. CT7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=2052574 {ECO:0000313|EMBL:PJI09771.1, ECO:0000313|Proteomes:UP000230839};
RN   [1] {ECO:0000313|EMBL:PJI09771.1, ECO:0000313|Proteomes:UP000230839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT7 {ECO:0000313|EMBL:PJI09771.1,
RC   ECO:0000313|Proteomes:UP000230839};
RA   Xin F., Chen T.;
RT   "The draft genome sequence of Clostridium sp. CT7, a unique bacterium
RT   capable of producing butanol from glycerol uncoupled acetone and 1,3-
RT   propanediol formation.";
RL   Submitted (NOV-2017) 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:0000256|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=5.6.2.4;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01452};
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_01452};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01452};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01452};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_01452};
CC   -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000256|HAMAP-
CC       Rule:MF_01452}.
CC   -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01452}.
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:PJI09771.1}.
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DR   EMBL; PETE01000002; PJI09771.1; -; Genomic_DNA.
DR   RefSeq; WP_066022629.1; NZ_PETE01000002.1.
DR   AlphaFoldDB; A0A2M8TFL3; -.
DR   OrthoDB; 9758506at2; -.
DR   Proteomes; UP000230839; Unassembled WGS sequence.
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-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: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; 3.90.320.10; -; 1.
DR   Gene3D; 6.10.140.1030; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   HAMAP; MF_01452; AddB_type1; 1.
DR   InterPro; IPR049035; ADDB_N.
DR   InterPro; IPR014140; DNA_helicase_suAddB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   NCBIfam; TIGR02773; addB_Gpos; 1.
DR   PANTHER; PTHR30591; RECBCD ENZYME SUBUNIT RECC; 1.
DR   PANTHER; PTHR30591:SF1; RECBCD ENZYME SUBUNIT RECC; 1.
DR   Pfam; PF21445; ADDB_N; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01452};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01452}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01452};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01452};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_01452}; Helicase {ECO:0000313|EMBL:PJI09771.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01452};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01452};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01452};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01452};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01452};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01452};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01452}; Reference proteome {ECO:0000313|Proteomes:UP000230839}.
FT   DOMAIN          5..287
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21445"
FT   DOMAIN          775..1114
FT                   /note="PD-(D/E)XK endonuclease-like"
FT                   /evidence="ECO:0000259|Pfam:PF12705"
FT   BINDING         786
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT   BINDING         1104
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT   BINDING         1107
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT   BINDING         1113
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
SQ   SEQUENCE   1153 AA;  133760 MW;  16A967BCAA1F5D6F CRC64;
     MSLRFIYGRA GSGKSQFCIN SIHSRIEKGG DKPLILVVPE QFSFQSEKSI LTLIGEKSLS
     RVRVISFKRM AYRVFDEVGG IAREHMNSSG KSMLFYHIMN KLKDEFKVFA LSARQKGFVD
     TVSDTISEFK KYELTPEILR STIDNVEDDE LKNKLHDLSL IYDEFDKLLH KNYIDSDDDL
     TMLKDKIKFS NMLSGAEIWL DEFSSFIPQQ YGIIEELLKK CSRVNITLTM DYGNVPYDDD
     IFSVTKNTEN RIMKIAQDNN VKIDKPVNLN KRPFYRFKRS PELGFLEKNL YSFPYEIYKS
     EPKKIGIFKT SNLYTEVEET ARKIVEFVRD KKMRYSDMAV VTGDLGSYKK TVAVIFKEYG
     IPFFIDENKD IEDNTLIILI KSIMDIFIKN WSYEAVFRYL KTGFTDVPYD DIDILENYVL
     AAGIKGKKKW TEKDWTYNVY HNGYDDEVSV ENQERLAKVN EIRNKVVEPI VEFRKKVLRK
     SNVAEICKSL FEFLCDINVP DKVEKMVSEF RESGRQVLAN EYSQIWNVII ELMDQLVEVM
     GDEKANLEQF SKIFSIGVKE HKMGLIPSSL DQVLVGSIDR LKSHAIKLIF IMGVNDGVFP
     SAAMEEGILS DRDREILMNS GVELAKDTKT QAMEQRFLVY TSIANSSEYL ILSYPIADYE
     GKTLRPSMII NRMKTLFPEL KEKSDVIKID NDDENMKLVS STVPTFNEMV ASFRKEVDGK
     NHSSAVWHDV YRWYCKDESW SQKCSNMFKA VAYTTQVDYI SEEKAVKLYG SSLKMSVSRL
     EKYVECPFSY YVQYGLNIKE RKMFSLTPPD LGSFMHKVID EFCENIREEN IEWKDVDDKV
     CEKKIYEIVD RELEDNAGSI FNSSPRYSYM TLRLKRILKR TARIVAEQFK RSGFRPAGYE
     VTFENGGNYP PITVKLADNS EVVLTGRIDR IDMLEKDGNT YIRIIDYKSG NKIFKLSDVY
     YGFDIQLLLY LDAILQSENL EDDDRTLPGG IFYFTMDDPI IKDKRNLTEE EIKEEIMKHL
     KMKGLLLSDP EVVHEMDRQM EGASILIPAS IKKDGTLGRS SAATKEQFEM LIGHVKNLVI
     KNCEKLLMGD IKIRPYKNGK EKPCDYCIYS SICRFDTMFH GNNYRYVKEK SDDEVFKLIG
     KEIDEEGDYN ERN
//
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