ID A0A2T1NBJ0_9FLAO Unreviewed; 815 AA.
AC A0A2T1NBJ0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:PSG89453.1};
GN ORFNames=C7H52_06675 {ECO:0000313|EMBL:PSG89453.1};
OS Aurantibacter aestuarii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aurantibacter.
OX NCBI_TaxID=1266046 {ECO:0000313|EMBL:PSG89453.1, ECO:0000313|Proteomes:UP000238426};
RN [1] {ECO:0000313|EMBL:PSG89453.1, ECO:0000313|Proteomes:UP000238426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 32269 {ECO:0000313|EMBL:PSG89453.1,
RC ECO:0000313|Proteomes:UP000238426};
RA Cheng H., Wu Y.-H., Guo L.-L., Xu X.-W.;
RT "Mesoflavibacter sp. HG37 and Mesoflavibacter sp. HG96 sp.nov., two marine
RT bacteria isolated from seawater of Western Pacific Ocean.";
RL Submitted (MAR-2018) 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:PSG89453.1}.
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DR EMBL; PXOQ01000008; PSG89453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1NBJ0; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000238426; 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 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; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 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:UP000238426};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 290..459
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 554..712
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 522..534
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 549..565
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 815 AA; 94424 MW; 363D455EEB908A0E CRC64;
MHFIDVILPI PLEKRFTYSI TKAESEFLQV GMRVAVPFGK SKVYTAIVAG IHTTAPLVYE
AKEIHQILDE TPLVSLKQLE LWAWISNYYL CSEGEVMRAA LPNAFLLESE TLVVKNTVKE
FDAASLKDDE FLVYEALQKS SSIKINELEA VLNKRNVLPV VKGLIEKSLI HLEEEIYEKY
KPKLVQYVKL HEQHLKEDQL QQLLETLSRA PKQREVVLSL FMMQSKSKLP FKVSDLSEQS
QASNQIIKTL IDKEVLQSYY IQTDRINFED DTTNSKHLNE EQSVALTQIL NQFETQNVVL
LHGVTSSGKT EVYVKLIENA LEKGEQVLYL LPEIALTTQL VNRLQNYFGE QVAVFHSKYT
IHERVEVYNN VLNSLDKAKI IIGARSSLFL PFSNLGLVIV DEEHEQSYKQ YDPAPRYHAR
DTAIVLAHMY KAKTLLGSAT PSIESYYNTQ IGKYGLVELK KRYNNVQLPD IELVDIKVKH
KRKLMNGHFS DRLIEEMELT LGEGLQVILF QNRRGYSPIV ECNTCGHAPQ CPNCDVSLTY
HHYRSQLRCH YCGYTMAMLQ KCMACYQPTL NTKGFGTEQI EQEVKSIFPK YKIARMDLDT
TRGKYGYEKI ITAFEQKETQ ILVGTQMLTK GLDFRNVKLV GIMNADNMLN FPDFRAHERS
FQLFQQVAGR AGRTDVQGKV LIQTYNPLHN ILQQVSEHHY LKMFNEQLQE RTNFKYPPFY
RLLKITFKHR DYNKVERSSE WFAKSLRQTF KQHILGPEFP PVSRIRNMYL KHVMIKIPQQ
QNLQKTKEVL LKINSSFQAI SDFKGVRVIF NVDYY
//
