ID A0A0R0DD46_9GAMM Unreviewed; 725 AA.
AC A0A0R0DD46;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 ORFNames=ABB28_04415 {ECO:0000313|EMBL:KRG75886.1};
OS Stenotrophomonas chelatiphaga.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=517011 {ECO:0000313|EMBL:KRG75886.1, ECO:0000313|Proteomes:UP000051386};
RN [1] {ECO:0000313|EMBL:KRG75886.1, ECO:0000313|Proteomes:UP000051386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21508 {ECO:0000313|EMBL:KRG75886.1,
RC ECO:0000313|Proteomes:UP000051386};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KRG75886.1}.
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DR EMBL; LDJK01000012; KRG75886.1; -; Genomic_DNA.
DR RefSeq; WP_057507464.1; NZ_LDJK01000012.1.
DR AlphaFoldDB; A0A0R0DD46; -.
DR PATRIC; fig|517011.3.peg.303; -.
DR Proteomes; UP000051386; Unassembled WGS sequence.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000051386};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 208..374
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT ZN_FING 433..445
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 460..476
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 725 AA; 78637 MW; AE6485AA1FF68928 CRC64;
MDAPLPTLRI ALPVPLPQLF DYLPPEGPAP DVVVGCRIRV PFGPRELVGV VVEQGSADPA
ASLRQALTWL DPAPLLQAEL WHSLQWLARY THAPLGEVLS TALPGPLRHG EPMPETHHWG
WQLSADGREQ RGSLRAGSRP RQLAELLADA VVDEDVIAAR MDDWRTAARS LAKRGLAERV
ALAVAPLQAS PLGGPTLNPE QANAVQAITA AQGFAPFLLD GVTGSGKTEV YLQAIIQCLA
QGRQALVLVP EIGLTPQTLA RFRGRLGIAV HAFHSGLNDN ERARVWAAAS RGEARVIVGT
RSAIFMPLPE AGLLIVDEEH DNSYKQQDGI RYHARDFALV RAKALGIPVV LGSATPAMET
LHNAHAGRFT HLRLKVRAGD AMPPRVRILD VRKRPLRDGL SPQVLEGIAE HLRNGQQVLV
FKNRRGYAPV LLCHDCGWTA PCQRCDAPMT VHGAGRRLQC HHCGARQAAP LACPACASLA
LQPQGIGTER LEEHLAQAFP DVPVLRIDRS TTSRRDALEQ QLARLGDQPG ILVGTQILAK
GHDLPKLTLV VVVGIDEGLF SSDFRATEKL AQQLIQVAGR AGRARDPGEV WLQTHHPGHP
LLETLVNGGY HPFAAAELNQ RQAAGFPPFA HLALLRAEAQ QVEHANAFLL AVRALVGEQP
HLEAFGPMPA PMPRRAGYQR TQLLLSSAQR PALHAVLDHV APLLQGLPEA RKVRWSLDVD
PVDLY
//
