GP1D_CHLT2
ID GP1D_CHLT2 Reviewed; 451 AA.
AC B0BCM3; P08781; P10555; P22445;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Probable plasmid replicative DNA helicase;
DE EC=3.6.4.12;
DE AltName: Full=DnaB-like protein;
DE AltName: Full=Protein P-3;
DE AltName: Full=Virulence plasmid protein pGP1-D;
GN OrderedLocusNames=pL2-03;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OG Plasmid pL2, and Plasmid pLGV440.
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pLGV440;
RX PubMed=2845228; DOI=10.1111/j.1365-2958.1988.tb00060.x;
RA Comanducci M., Ricci S., Ratti G.;
RT "The structure of a plasmid of Chlamydia trachomatis believed to be
RT required for growth within mammalian cells.";
RL Mol. Microbiol. 2:531-538(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B; PLASMID=pL2;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
CC -!- FUNCTION: Required for growth within mammalian cells.
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=3.6.4.12;
CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000305}.
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DR EMBL; X07547; CAA30421.1; -; Genomic_DNA.
DR EMBL; AM886278; CAP09061.1; -; Genomic_DNA.
DR PIR; S01921; S01921.
DR RefSeq; YP_001654084.1; NC_010286.1.
DR AlphaFoldDB; B0BCM3; -.
DR SMR; B0BCM3; -.
DR OMA; YPSIDEH; -.
DR Proteomes; UP000000795; Plasmid pL2.
DR GO; GO:1990077; C:primosome complex; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR CDD; cd00984; DnaB_C; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR InterPro; IPR007693; DNA_helicase_DnaB-like_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00772; DnaB; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48024; SSF48024; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Plasmid; Primosome.
FT CHAIN 1..451
FT /note="Probable plasmid replicative DNA helicase"
FT /id="PRO_0000391798"
FT DOMAIN 194..451
FT /note="SF4 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT BINDING 225..232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
SQ SEQUENCE 451 AA; 51457 MW; 2CD73A152C72A1F1 CRC64;
MKTRSEIENR MQDIEYALLG KALIFEDSTE YILRQLANYE FKCSHHKNIF IVFKYLKDNG
LPITVDSAWE ELLRRRIKDM DKSYLGLMLH DALSNDKLRS VSHTVFLDDL SVCSAEENLS
NFIFRSFNEY NENPLRRSPF LLLERIKGRL DSAIAKTFSI RSARGRSIYD IFSQSEIGVL
ARIKKRRATF SENQNSFFDA FPTGYKDIDD KGVILAKGNF VIIAARPSIG KTALAIDMAI
NLAVTQQRRV GFLSLEMSAG QIVERIIANL TGISGEKLQR GDLSKEELFR VEEAGETVRE
SHFYICSDSQ YKLNLIANQI RLLRKEDRVD VIFIDYLQLI NSSVGENRQN EIADISRTLR
GLASELNIPI VCLSQLSRKV EDRANKVPML SDLRDSGQIE QDADVILFIN RKESSSNCEI
TVGKNRHGSV FSSVLHFDPK ISKFSAIKKV W