ID E1LLK4_STRMT Unreviewed; 763 AA.
AC E1LLK4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN Name=pcrA {ECO:0000313|EMBL:EFN98894.1};
GN ORFNames=SMSK564_0705 {ECO:0000313|EMBL:EFN98894.1};
OS Streptococcus mitis SK564.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=585203 {ECO:0000313|EMBL:EFN98894.1, ECO:0000313|Proteomes:UP000004966};
RN [1] {ECO:0000313|EMBL:EFN98894.1, ECO:0000313|Proteomes:UP000004966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK564 {ECO:0000313|EMBL:EFN98894.1,
RC ECO:0000313|Proteomes:UP000004966};
RA Daugherty S.C., Tallon L.J., Jones K.M., Liu X., Kilian M., Tettelin H.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU364053};
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, ECO:0000256|RuleBase:RU364053}.
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:EFN98894.1}.
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DR EMBL; AEDU01000009; EFN98894.1; -; Genomic_DNA.
DR RefSeq; WP_000992906.1; NZ_AEDU01000009.1.
DR AlphaFoldDB; E1LLK4; -.
DR eggNOG; COG0210; Bacteria.
DR Proteomes; UP000004966; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; 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; IPR005751; ATP-dep_DNA_helicase_PcrA.
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 NCBIfam; TIGR01073; pcrA; 1.
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}; DNA-binding {ECO:0000256|RuleBase:RU364053};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 6..284
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 285..566
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 763 AA; 85835 MW; 4986952C8F409741 CRC64;
MNALLNGMND RQAEAVQTTE GPLLIMAGAG SGKTRVLTHR IAYLIDEKMV NPWNILAITF
TNKAAREMKE RAYSLNPATQ DCLIATFHSM CVRILRRDAD HIGYNRNFTI VDPGEQRTLM
KRILKQLNLD PKKWNERSIL GTISNAKNDL IDDVAYAAQA GDMYTQIVAQ CYTAYQKELR
QSESVDFDDL IMLTLRLFDQ NPDVLTYYQQ KFQYIHVDEY QDTNHAQYQL VKLLASRFKN
ICVVGDADQS IYGWRGADMQ NILDFEKDYP QAKVVLLEEN YRSTKTILQA ANEVIKNNKN
RRPKNLWTQN ADGEQIVYYR ANDELDEAVF VAKTIDELGR SQNFLHKDFA VLYRTNAQSR
TIEEALLKSN IPYTMVGGTK FYSRKEIRDI IAYLNLIANL SDNISFERII NEPKRGIGPG
TVEKIRDFAN VQDMSMLDAS ANIMLSGIKG KAAQSIWDFA NMILDLREQL DQLSITELVE
EVLEKTGYID ILNVQATLES KARVENIEEF LSVTKNFDDT SDVPEEETGL DKLSRFLNDL
ALIADTDSGS QETSEVTLMT LHAAKGLEFP VVFLIGMEEN VFPLSRAAED QDELEEERRL
AYVGITRAEK ILYLTNANSR LLFGRTNYNR PTRFINEISS DLLEYQGLAR PANTSFKASY
SSGGVAFGQG MSLAQALQDR KRSAAPKTIQ SSGLPFGQFT AGAKSASSEA NWSIGDIALH
KKWGEGTVLE VSGSGATQEL KINFPDVGLK KLLASVAPIE KKI
//
