ID D2UG39_XANAP Unreviewed; 729 AA.
AC D2UG39;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
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:0000313|EMBL:CBA17350.1};
GN Synonyms=priA {ECO:0000256|HAMAP-Rule:MF_00983};
GN OrderedLocusNames=XALc_2873 {ECO:0000313|EMBL:CBA17350.1};
OS Xanthomonas albilineans (strain GPE PC73 / CFBP 7063).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA17350.1, ECO:0000313|Proteomes:UP000001890};
RN [1] {ECO:0000313|EMBL:CBA17350.1, ECO:0000313|Proteomes:UP000001890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890};
RX PubMed=20017926; DOI=10.1186/1471-2164-10-616;
RA Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R., Cociancich S.,
RA Couloux A., Darrasse A., Gouzy J., Jacques M.A., Lauber E., Manceau C.,
RA Mangenot S., Poussier S., Segurens B., Szurek B., Verdier V., Arlat M.,
RA Rott P.;
RT "The complete genome sequence of Xanthomonas albilineans provides new
RT insights into the reductive genome evolution of the xylem-limited
RT Xanthomonadaceae.";
RL BMC Genomics 10:616-616(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FP565176; CBA17350.1; -; Genomic_DNA.
DR RefSeq; WP_012917343.1; NC_013722.1.
DR AlphaFoldDB; D2UG39; -.
DR STRING; 380358.XALC_2873; -.
DR GeneID; 57878181; -.
DR KEGG; xal:XALC_2873; -.
DR PATRIC; fig|29447.3.peg.2833; -.
DR eggNOG; COG1198; Bacteria.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000001890; 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; cd17929; DEXHc_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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000001890};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 207..373
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT ZN_FING 432..444
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 464..480
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 729 AA; 78808 MW; 7A1242F609F5BD10 CRC64;
MPAPAVTLRV ALPLPLPQLF DYLPPQGSAP SQGDIGRRVQ VPFGNRQMSG VVAALGEAEH
SPGLRAALAW LDPVPLLHGE LADSLRWLAR YSHAPLGEVL ATALPVTLRR GEPLPDTHAW
AWRLTEAGAG HRTRPGTRPH RLAELLAPGP LHEEQLDQAM HDWRSAARAL AKRDHAERIA
VPADASAPQP QTGPMANPEQ QAAIDTLHAT QGFAAFLLDG VTGSGKTEVY LQAIAACLAR
GRQALVLVPE IGLTPQTLAR FRARLGVPVH ALHSGLNDNE RARVWTAAWR GEAWVVVGTR
SAVFVPLPQA GLIVIDEEHD GSYKQQDGIR YHARDFALVR AKALDVPVLL GSATPSLESL
HNANSGRYTH LRLTHRAGDA RPPTVRVLDV RKRPLQDGLS PEVLTGIGAT LAEGGQVLVF
KNRRGYAPVL LCHDCGWTAP CQRCSTPLHT TPMTVHAGGR RLQCHHCGAR QPAPLACPDC
GSLALQPQGI GTERLEERLV HAFPEVPVLR IDRGTTQRRD GLETQLATLG NAPGILVGTQ
ILAKGHDLPQ LSRVVVVGID EGLFSADFRA SEKLAQQLIQ VAGRAGRATR PGDVWLQTHH
PGHPLLEILV HGGYHAFAAA ELAQREAAGF PPFAHLALLR AEAKQVDHAN AFLAAVRALL
PAHDQVQRFG PMPAPMPRRA GFQRTQLLLS ASTRRALHRL LDAAVPAIHA LTQARRVRWS
LDVDPQDLY
//
