ID A0A5P1B158_ACIJU Unreviewed; 746 AA. AC A0A5P1B158; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 03-MAY-2023, entry version 11. 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=F4T90_02930 {ECO:0000313|EMBL:MQZ56395.1}; OS Acinetobacter junii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter. OX NCBI_TaxID=40215 {ECO:0000313|EMBL:MQZ56395.1, ECO:0000313|Proteomes:UP000380195}; RN [1] {ECO:0000313|EMBL:MQZ56395.1, ECO:0000313|Proteomes:UP000380195} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AMA32 {ECO:0000313|EMBL:MQZ56395.1, RC ECO:0000313|Proteomes:UP000380195}; RA Maria R.S., Adams M.D.; RT "Distinct mechanisms of dissemination of NDM-1 metallo-beta-betalactamase RT in Acinetobacter species spp. in Argentina."; RL Submitted (SEP-2019) 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:MQZ56395.1}. 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; VYTC01000004; MQZ56395.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5P1B158; -. DR Proteomes; UP000380195; 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 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 SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR TIGRFAMs; TIGR00595; priA; 1. 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 Zinc {ECO:0000256|HAMAP-Rule:MF_00983}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}. FT DOMAIN 225..391 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 486..643 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT ZN_FING 450..462 FT /note="C4-type" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983" FT ZN_FING 478..494 FT /note="C4-type" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983" SQ SEQUENCE 746 AA; 84657 MW; 3C52011BEE8DF6B3 CRC64; MNKANMPTEN SNAILYRIRV ALPVYVYDTF DYTVSAEQYL QAQIGARVSV SFGRQNLIGI ITEKVDPNEP FTGQFKLKPI TALLDEDAIL DQQVLTLLTW SAQYYQFPIG EVMQSALPAL LRQGRALDIL FHHWNILTHD DPESLLKRSQ KQYDAYQILK LHPHGATENI LNLSGVETAT LKALEKKGLI ECQLEAHDFT PMPIQLAQMP LTPNEDQKRA IQQILKAQQR YQAFLLDGLT GSGKTEVYLQ VMHEVLKQGK QVLVLVPEIG LTPQTVARFK SRFHCDVALL HSGLNDSKRL QAWQHAQTGK ASIIIGTRSA IYTPLPHLGL IILDEEHDLS YKQQEGFRYH TRDVALYRGH LHNCPVILGS ATPSIDSYYL VESGKLHLLE LNQRAGTAVL PKMHVIDLKV AKKKNGISQN LIDQIKLTLE RKEQVLIFLN RRGYAPVLLC ESCGWQANCP HCDAHFTVHS QPYSYLHCHH CGTINRLPDE CPACKHQTLK SIGAGTAKVE EQLHELFPHH EVIRVDRDST SRVGSWQKIY DRIQQNKPSI LLGTQMLAKG HHFPHVTLVA ILDIDSGLLS VDPRAPERTA QLIIQVAGRA GRGEHKGSVY LQSLRPDHPM LTTLIEQDYR AVAKQMLSER KVAMLPPYRY AVLVRVESKD RDYSQQFLME AAQGLRAIAA DIIEIWGPIP APMERKAGRY RAHMVILSAD RAKLHFYLRQ WWQQVVHLPR QHQLRLSIDV DPQEFS //