ID J9ZD29_LEPFM Unreviewed; 746 AA.
AC J9ZD29;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN Name=pcrA {ECO:0000313|EMBL:AFS54264.1};
GN OrderedLocusNames=LFML04_2068 {ECO:0000313|EMBL:AFS54264.1};
OS Leptospirillum ferriphilum (strain ML-04).
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=1048260 {ECO:0000313|EMBL:AFS54264.1, ECO:0000313|Proteomes:UP000006177};
RN [1] {ECO:0000313|EMBL:AFS54264.1, ECO:0000313|Proteomes:UP000006177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML-04 {ECO:0000313|EMBL:AFS54264.1,
RC ECO:0000313|Proteomes:UP000006177};
RX PubMed=22203551; DOI=10.1007/s12275-011-1099-9;
RA Mi S., Song J., Lin J., Che Y., Zheng H., Lin J.;
RT "Complete genome of Leptospirillum ferriphilum ML-04 provides insight into
RT its physiology and environmental adaptation.";
RL J. Microbiol. 49:890-901(2011).
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};
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|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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DR EMBL; CP002919; AFS54264.1; -; Genomic_DNA.
DR RefSeq; WP_014961768.1; NC_018649.1.
DR AlphaFoldDB; J9ZD29; -.
DR STRING; 1048260.LFML04_2068; -.
DR KEGG; lfi:LFML04_2068; -.
DR PATRIC; fig|1048260.3.peg.2251; -.
DR HOGENOM; CLU_004585_5_2_0; -.
DR OMA; HCANILI; -.
DR Proteomes; UP000006177; 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:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF21196; PcrA_UvrD_tudor; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|PROSITE-ProRule:PRU00560,
KW ECO:0000313|EMBL:AFS54264.1};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 4..281
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 282..562
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 621..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 746 AA; 84571 MW; 7E742219D345F9A3 CRC64;
MTREELNPAQ QEAVSHEGGP LLVLAPAGSG KTRVVIARLL YLLDRYGWSE ERLLVVTFTR
KAARELLHRI SRLRPSSRPS WVGTFHSVAA RMLRQHAERV DLPREFTIVD GPDQLQMIRD
LLGRQGLSDK EVDPKKLAGR IGKWKSAGVD PAEAIRTSFG PFRIQAELYA AYQDNLALQK
ALDFDDLLLT LVRCLEQDPE VRESYQRQFE HILVDEYQDT NPLQERLLRL LSRDRQNVTV
VGDDDQSIYR FRGAEVGHIL SFPKEYPGAR QVVLTVNYRS TRPIVTAASS MISSALARYR
KDMVSTGRPG EPVFLKKLDS EWAEARFVAR TIREKVERGA MFRDQVVLFR MNVQAQPFVR
AFSEAGIPFQ TRGAVQGFFN RREIRDLLAY LRVSANPFDR ISLGRILNIP PRGMGAKARE
RLDQQAGNPG LSSWELLERL SLDLSGKARE SARAFANDLQ EASRMARGGD GPLSLLQFWL
SRTGYEKWVS EEEAGEDAPG REENLKELLR MSERFGNGIG ELTDRTPTGV FLEELALSQE
DPGEPGESPD RVSLLTIHQA KGLEFPHVYL VGAEEDILPM KSREKVDVEE ERRLFYVAMT
RARDSLVITW CLTRQLFGRT ESPRPSRFLR DIPPEAFQGD RPVFRPETSA PRQTSESFQR
KFFSPPPLAP SRPGRDFRPV PEKGSPTPTG VLRPEWIGKT VVHPRFGRGR VEEAYGEGGD
LELSIRFESS GVRRLLERFA NLQVDG
//