ID W8U3L7_PEPAC Unreviewed; 1161 AA.
AC W8U3L7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN Name=addB {ECO:0000313|EMBL:AHM55581.1};
GN ORFNames=EAL2_c02780 {ECO:0000313|EMBL:AHM55581.1};
OS Peptoclostridium acidaminophilum DSM 3953.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptoclostridium.
OX NCBI_TaxID=1286171 {ECO:0000313|EMBL:AHM55581.1, ECO:0000313|Proteomes:UP000019591};
RN [1] {ECO:0000313|EMBL:AHM55581.1, ECO:0000313|Proteomes:UP000019591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3953 {ECO:0000313|EMBL:AHM55581.1,
RC ECO:0000313|Proteomes:UP000019591};
RX PubMed=24926057;
RA Poehlein A., Andreesen J.R., Daniel R.;
RT "Complete Genome Sequence of Amino Acid-Utilizing Eubacterium
RT acidaminophilum al-2 (DSM 3953).";
RL Genome Announc. 2:e00573-14(2014).
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};
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DR EMBL; CP007452; AHM55581.1; -; Genomic_DNA.
DR AlphaFoldDB; W8U3L7; -.
DR STRING; 1286171.EAL2_c02780; -.
DR KEGG; eac:EAL2_c02780; -.
DR PATRIC; fig|1286171.3.peg.215; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OrthoDB; 9758506at2; -.
DR Proteomes; UP000019591; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase 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:InterPro.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR049035; ADDB_N.
DR InterPro; IPR014140; DNA_helicase_suAddB.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
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 Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000313|EMBL:AHM55581.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AHM55581.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000019591};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..314
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21445"
FT DOMAIN 325..667
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13361"
FT DOMAIN 785..1125
FT /note="PD-(D/E)XK endonuclease-like"
FT /evidence="ECO:0000259|Pfam:PF12705"
SQ SEQUENCE 1161 AA; 131050 MW; 12E818892582EA8E CRC64;
MEKPCNMPLC LRFVAGFFGI IGTGVLIFGR GGIMHIKYVV SRAGRGKTSA VYGDIKKCMN
ENKDVKLVLM VPEQFTLQAE TDIIGALGSE GIMQLEVLSF QRLAHRILSE VGGIKRVQIN
QSGKAMLLRS IIDANSDELT LYARASKQEG FLSKCSALID DLKRQDVDPQ SLIMCSEALG
DSMLRLKLRE IGFIYEKYTR ALEEGYADEH DWLRLLARKI DSSHLLEGAH VWIDGFSGFS
AGELSVINEL VKKASEVSVS LTLDLEAGPD YELFAATRRT MKAISAAARE AGAGESILRA
RLESAKPPEL LHLERNLYAY PAARYAGDTD GIRMFAGSSR HSEVENAAVE IIKLASGNGY
RWRDIAIVTG ALEDYAQIIK RTFSEYGIPV FIDEKRPITN NPIIRFILAA LDIAARDFRY
EDVFKFIKTG FTELGRGSWE NLENYALRYG IKSSAWMREF TLGSDDERTM AEEARKKLVP
PLAGLKKKLG KKKTVKDFTR ILYDFMVELD MPEKIENWTQ MLMDDSRLEY VNENTQIWNI
VIEIFDQMVE MMGDLKVDLR EYAGILSAGF AEHRIGIIPP TMDQVIAGSL ERSKSHEIKA
LFVLGVNDGV LPSGFSDEEL ILDDEKLLMK EHGVHISTDS ITRAEEERFS IYTSLSKPSG
ILYMSYAIAD EEGKALRPSI IADRMKKLYG GLVTESDIVV DSSRRLEMLV APLPGLRQLS
ELIRQEMDTA IEDGLWRDLY SWYTSREQWS EKADIVCKGL FHKNQQDYIG AGLAARLYPS
PLKSSISRLE RFANCPFAHF VNYGLSPRER LEYTVSMPDM GTLFHSSVEK FSKEISSENI
NWRELEQQKS DAIVERVIDS MVPEFGSGVF YSSHRYSYLV NKIKRVGKRA AWAIVEHIRR
GEFEPMDHEV EFSEKGSIPA IIIELPGGES IELEGRIDRV DIFGDEKQGY VKIIDYKSGS
KKFTLSDAYY GLQIQLLVYM DALLENKQLL EFDELHPAGV FYFRIDDPFI DAEKLGETDI
EKGILKQLKM NGIVLRDVSV VKAMDSEIES ERFSSIIPAE VKNDGELSER SSAVSEEEFR
RLIGHVKNLI REIGAEIIKG KIRIQPCRSG SEISCGYCKF KSICQFDTLL EDNEYRNIRK
LSDGQVRGLI SGKGHSDDKV D
//
