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Database: UniProt
Entry: K4IKY2_BIFAP
LinkDB: K4IKY2_BIFAP
Original site: K4IKY2_BIFAP 
ID   K4IKY2_BIFAP            Unreviewed;      1346 AA.
AC   K4IKY2;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   OrderedLocusNames=BAST_0415 {ECO:0000313|EMBL:AFU71009.1};
OS   Bifidobacterium asteroides (strain PRL2011).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1147128 {ECO:0000313|EMBL:AFU71009.1, ECO:0000313|Proteomes:UP000007006};
RN   [1] {ECO:0000313|EMBL:AFU71009.1, ECO:0000313|Proteomes:UP000007006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRL2011 {ECO:0000313|EMBL:AFU71009.1,
RC   ECO:0000313|Proteomes:UP000007006};
RX   PubMed=23028506; DOI=10.1371/journal.pone.0044229;
RA   Bottacini F., Milani C., Turroni F., Sanchez B., Foroni E., Duranti S.,
RA   Serafini F., Viappiani A., Strati F., Ferrarini A., Delledonne M.,
RA   Henrissat B., Coutinho P., Fitzgerald G.F., Margolles A., van Sinderen D.,
RA   Ventura M.;
RT   "Bifidobacterium asteroides PRL2011 genome analysis reveals clues for
RT   colonization of the insect gut.";
RL   PLoS ONE 7:E44229-E44229(2012).
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; CP003325; AFU71009.1; -; Genomic_DNA.
DR   RefSeq; WP_015021448.1; NC_018720.1.
DR   STRING; 1147128.BAST_0415; -.
DR   GeneID; 41009689; -.
DR   KEGG; bast:BAST_0415; -.
DR   PATRIC; fig|1147128.3.peg.424; -.
DR   eggNOG; COG0210; Bacteria.
DR   eggNOG; COG2887; Bacteria.
DR   HOGENOM; CLU_003630_0_0_11; -.
DR   Proteomes; UP000007006; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 5.
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; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF55; DNA HELICASE; 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   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}.
FT   DOMAIN          2..423
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          424..770
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          211..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         23..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1346 AA;  147754 MW;  610B36915FFAB4CC CRC64;
     MKQTAEQSAI VDADVNEDLL VVAGAGSGKT MTMTSRIIAL IRRGVPSEQI LGLTFTRKAA
     SELQSRVGSA VIRRDQGRGT SGVDPERNFL KPTVSTYDAF FQSIVRQYGL LVGMDQDTRP
     LSSAGAYQLA SQVVADHLDL IFPAGASAQD GDSGDLGSAT FSTTVNRVLG LTGAVTTSMI
     SSDCPDFDQA VDRIRAWDRV FVDRADQLIG DQPVPATEPR VSQTPPKRSK KETDEHYQGK
     IKDFQDTRRS IRIYRVDAMR RAVLTREKLL TLVQDYQRAK RRANMAEFGD FTLAAFQLVE
     RFPSISAQLR RRYSHVFLDE YQDTSTTQAL LLAAIFHPHN RQEDQGSEDQ APGRSAVTAV
     GDPFQSIYAW RGASPGAFRT FQAQFGMLAD RPDFGGGPLS GVTAFGRSQD QDPLTLSRTF
     RNSGWVLKAA NQLTVPLRHR GRESRSEAEL REVDVAKLRP REDADPGTVG LLGYATGGQE
     IDGVVRFALR ARELYGNQGD APHVAVLFRS KAALPRYREA MEAAGLSCQV VGYSSLFDRP
     EVMDLRALLS LVCDHTDSDS LMRLLASARF GMDAADLSAL ASLAAKVNED SQYRALVRAG
     LVESDSDPRR RREDLHRYRD QVPNDVFLVD LLLRDDLPDL LKSSGLSARG RVLAAEAARV
     VCQVQAESSA PLRQVVIAAI RALNLDVDLV LARSLADPER PLEPSQAKAG IQALLDQVDV
     YLSELPQGIG PSLRGFVSWL SSLDQSPEMP TDGDDRQADV ALMTVHQAKG LEWDAVAVVG
     LKRGAFPSSQ GDRLTVKPAL DQPVVQSPDG PVYQYNCTAR TWLVDPESVP VPVRADAMIL
     PRFPHDAPLG ADPEDLLGRL DLASLEEEAT GLSRESWLDD QAQPVRADAI APSQREQYGR
     RLLDDERRLI YVAATRARHD LLLTFSQDSQ AESAALNTPA PDPDKASNFW TELVELFQEE
     PEAVKLEQAE DAQEGEPTPP LGLFVGENAQ SYRQAVVDQA LEEVDQVAAR DGGRDQALWP
     PVLSARTREA LNRSASWVRA GKPGDPVIDE EGDDGLYANA VRVLQVSTGR LGVANDQLLT
     DLDLLRRTGR RILGHGASSV TAIQAGSAGG DPKMERDYWQ GLVRPIPQVA SPQAEAGTRF
     HDWARRFILP EISAPQGLVD LPDQAEAPNL LDGPLGPGAM AERARMLAGL DRERESMDSQ
     ADPVQARLLT WEQRLAESEW AQRTPVWVER PIVAVLAGRI VKGKLDAVFA GGLDPDRPDL
     HYTIVDWKTG SRPRGEDSTN RRLVQLDFYR LLLSRLEGIG LSTIDACLYY VSEDRPQDRL
     IRARARTEEE ILASMAEGIP EQSDED
//
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