ID A0A174VZG3_9CLOT Unreviewed; 735 AA.
AC A0A174VZG3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=CP373A1_06895 {ECO:0000313|EMBL:OBY11216.1};
OS Clostridium paraputrificum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=29363 {ECO:0000313|EMBL:OBY11216.1, ECO:0000313|Proteomes:UP000092714};
RN [1] {ECO:0000313|EMBL:OBY11216.1, ECO:0000313|Proteomes:UP000092714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=373-A1 {ECO:0000313|EMBL:OBY11216.1,
RC ECO:0000313|Proteomes:UP000092714};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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:OBY11216.1}.
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DR EMBL; MAPZ01000016; OBY11216.1; -; Genomic_DNA.
DR RefSeq; WP_027097486.1; NZ_RAYJ01000004.1.
DR AlphaFoldDB; A0A174VZG3; -.
DR GeneID; 42775321; -.
DR eggNOG; COG1198; Bacteria.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000092714; 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:UP000092714};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 212..378
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 474..633
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 440..452
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 466..482
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 735 AA; 84599 MW; 1796B3F6DA3C50C7 CRC64;
MFELYAEVII NSDAIEIDRP FTYKVKEELL DIIEIGHRVK VPFGVKNKPT EAFVLGLKCE
GIENVKKIKY ISSILDDIPI LTRDDLKLVD FLRENYLCKY IDAIRTIIPS GLSKGIKNKK
KTVIVFNKEL DGKLKDKDNY VKIVNLIKEK DGELTKSEII NDYSLSSYSL NKLIENGYLL
TEDRVVYRYN TRSYIEESKN VLNDEQKNAF NKILNSDKKG FLLKGVTGSG KTEVYMNLVG
ETLKEGKSAI VLVPEISLTP QMIERFKGRF GKNVALFHSK LSQGERFDEW YRIKKGEARL
VVGARSAIFL PLDNLGIIII DEEHENTYKS EQNPKYLTKE VAKFLSEIKG CKYILGSATP
SIETYYEALN GKLELVEIKN RVSNRPLPQM EIVDMREELK SRNLSLLSRS LYNEMKETLE
RKEQIILFLN RRGFSSFVSC RSCGYVFKCP ECDLSMTYHK NGYLICHYCG RAQREQKVCP
ECGSKYVKFF GAGTQRVEEE VKKYFPKARV MRMDVDTTRN KDSHENIYNA FKSGEGDVLI
GTQMVSKGLD FKNVTLVGVL AADISLNIPD YRSSERTYQI ITQVAGRAGR GEKKGKVVIQ
TYTPNSLSLQ YAIENNYNDL YNEEIKVRKI MNYPPFSTIF LINSISKDER KLKEFMNKVG
ESLRKLLDSR ENIQILGPVP CIITKLKDNY RWQIIIKGNL DNKLKLKIKD ILYELNKSVY
NEIRISMDIN PNNMT
//
