ID K0PAC3_9BACT Unreviewed; 803 AA.
AC K0PAC3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Primosomal protein N' {ECO:0000256|HAMAP-Rule:MF_00983};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00983};
DE AltName: Full=ATP-dependent helicase PriA {ECO:0000256|HAMAP-Rule:MF_00983};
GN Name=priA {ECO:0000256|HAMAP-Rule:MF_00983,
GN ECO:0000313|EMBL:CCM10450.1};
GN ORFNames=CAHE_0673 {ECO:0000313|EMBL:CCM10450.1};
OS Cardinium endosymbiont cEper1 of Encarsia pergandiella.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Amoebophilaceae;
OC Cardinium.
OX NCBI_TaxID=1231626 {ECO:0000313|EMBL:CCM10450.1, ECO:0000313|Proteomes:UP000003996};
RN [1] {ECO:0000313|EMBL:CCM10450.1, ECO:0000313|Proteomes:UP000003996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zchori-Fein et al. 2004 {ECO:0000313|Proteomes:UP000003996};
RX PubMed=23133394; DOI=10.1371/journal.pgen.1003012;
RA Penz T., Schmitz-Esser S., Kelly S.E., Cass B.N., Muller A., Woyke T.,
RA Malfatti S.A., Hunter M.S., Horn M.;
RT "Comparative Genomics Suggests an Independent Origin of Cytoplasmic
RT Incompatibility in Cardinium hertigii.";
RL PLoS Genet. 8:e1003012-e1003012(2012).
CC -!- FUNCTION: Involved in the restart of stalled replication forks.
CC Recognizes and binds the arrested nascent DNA chain at stalled
CC replication forks. It can open the DNA duplex, via its helicase
CC activity, and promote assembly of the primosome and loading of the
CC major replicative helicase DnaB onto DNA. {ECO:0000256|HAMAP-
CC Rule:MF_00983}.
CC -!- SUBUNIT: Component of the primosome. {ECO:0000256|HAMAP-Rule:MF_00983}.
CC -!- SIMILARITY: Belongs to the helicase family. PriA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00983}.
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DR EMBL; HE983995; CCM10450.1; -; Genomic_DNA.
DR RefSeq; WP_014934817.1; NC_018605.1.
DR AlphaFoldDB; K0PAC3; -.
DR STRING; 1231626.CAHE_0673; -.
DR KEGG; che:CAHE_0673; -.
DR PATRIC; fig|1231626.3.peg.659; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_1_1_10; -.
DR OrthoDB; 9759544at2; -.
DR BioCyc; CEND1231626:AL022_RS03080-MONOMER; -.
DR Proteomes; UP000003996; Chromosome.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd18804; SF2_C_priA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.1440.60; PriA, 3(prime) DNA-binding domain; 1.
DR HAMAP; MF_00983; PriA; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005259; PriA.
DR InterPro; IPR041222; PriA_3primeBD.
DR InterPro; IPR042115; PriA_3primeBD_sf.
DR InterPro; IPR041236; PriA_C.
DR InterPro; IPR040498; PriA_CRR.
DR NCBIfam; TIGR00595; priA; 1.
DR PANTHER; PTHR30580; PRIMOSOMAL PROTEIN N; 1.
DR PANTHER; PTHR30580:SF0; PRIMOSOMAL PROTEIN N; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF17764; PriA_3primeBD; 1.
DR Pfam; PF18074; PriA_C; 1.
DR Pfam; PF18319; PriA_CRR; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00983}; DNA replication {ECO:0000256|HAMAP-Rule:MF_00983};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00983};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_00983};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00983};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00983};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00983};
KW Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 278..445
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT ZN_FING 508..520
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 535..551
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 803 AA; 91216 MW; EC50CD77AA1202F7 CRC64;
MKKFVDIIFP LPIKALTYSI PFQYQDRLEI GSSVLVPLRS SKLLLGIVIR CHNIPPSYPT
KDVLAISYAT PLFTTQQLAF LEWMANYYLS NLGETLSMAW PKILNNNIGF QYKESMGNYT
LSAIEQIIIT ALQHQSLSYR SIVSLIGQKD TNKALIALLS KRLVEATVET VIDPAERDNR
YITLSPTIHL DPFTITKLAP RSPKQQALLA HFLPNKENFP LYISKEVLLG YSQSAFHALY
KKGILIKTDS PQLVTFTAPC TPLSTLTTYQ KKALIEIERQ FTQKTAVLLY GTIGSGKTAL
YMHLIASALC QQKQVLFLVP EIGLITHMVE RIRPFWGEWL MVHHSKQSNK EGLKTWARLL
NPAALLVIGT RSALLLPFKA LQLIIIDEEH DQAYKQIDRM PTYHARESSI LLAQQHQAKV
LLGSATPSIE SYYNSQTGKY GLVRLSHRFG TAGQPKLFFI DLNIEKKRKA MRENFSLTLL
SKLEKNHIEG GQAMIFQNRR GYASYFLCAA CGWIPRCLTC SVSLTYHQAS NHLRCHYCDY
TRLTFSTCDH CGSKQLHNIG FGTEKLEESL QLIFPKQKMG RMDLDSTKGK NSYQSLLKKI
NDGSIDILVG TQMMAKGLDF ANMRLIGIPD IDGLLYFPDF RSNEKCFQLI TQLAGRAGRR
DKEGSVFIQT RQSDHPLFQY LSNGDYEGMY HSELAERKRF LYPPYVRLIK LRLSGMDGST
LQSGAIKLKK ILEKNFEGIA LGPQQPLVGK IRNYFLLDLL LKIPSKNLSR LQRIKEDVRN
GCKYMLSKEP YSKIKIVLDI DPI
//
