ID B2ULA1_AKKM8 Unreviewed; 738 AA. AC B2ULA1; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 22-JUL-2015, entry version 57. 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 OrderedLocusNames=Amuc_0043 {ECO:0000313|EMBL:ACD03890.1}; OS Akkermansia muciniphila (strain ATCC BAA-835 / Muc). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Akkermansiaceae; Akkermansia. OX NCBI_TaxID=349741 {ECO:0000313|EMBL:ACD03890.1, ECO:0000313|Proteomes:UP000001031}; RN [1] {ECO:0000313|Proteomes:UP000001031} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-835 / Muc {ECO:0000313|Proteomes:UP000001031}; RX PubMed=21390229; DOI=10.1371/journal.pone.0016876; RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M., RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.; RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin RT degrader, and its use in exploring intestinal metagenomes."; RL PLoS ONE 6:E16876-E16876(2011). 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- CC Rule:MF_00983}. CC -!- SIMILARITY: Belongs to the helicase family. PriA subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00983}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000256|HAMAP-Rule:MF_00983}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. 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; CP001071; ACD03890.1; -; Genomic_DNA. DR RefSeq; WP_012419105.1; NC_010655.1. DR ProteinModelPortal; B2ULA1; -. DR STRING; 349741.Amuc_0043; -. DR EnsemblBacteria; ACD03890; ACD03890; Amuc_0043. DR KEGG; amu:Amuc_0043; -. DR PATRIC; 20832556; VBIAkkMuc16855_0050. DR eggNOG; COG1198; -. DR HOGENOM; HOG000037414; -. DR KO; K04066; -. DR OMA; QRFNAPV; -. DR OrthoDB; EOG6KT2K4; -. DR BioCyc; AMUC349741:GHZ7-46-MONOMER; -. DR Proteomes; UP000001031; Chromosome. DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. 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-HAMAP. DR Gene3D; 3.40.50.300; -; 3. 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 Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 3. 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|HAMAP-Rule:MF_00983, KW ECO:0000256|RuleBase:RU000452}; KW Complete proteome {ECO:0000313|Proteomes:UP000001031}; KW DNA replication {ECO:0000256|HAMAP-Rule:MF_00983}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00983}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_00983, KW ECO:0000256|RuleBase:RU000452}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00983, KW ECO:0000256|RuleBase:RU000452}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00983}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00983, KW ECO:0000256|RuleBase:RU004294}; KW Primosome {ECO:0000256|HAMAP-Rule:MF_00983}; KW Reference proteome {ECO:0000313|Proteomes:UP000001031}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}. FT DOMAIN 214 383 Helicase ATP-binding. {ECO:0000256|HAMAP- FT Rule:MF_00983}. FT DOMAIN 459 635 Helicase C-terminal. {ECO:0000256|HAMAP- FT Rule:MF_00983}. FT NP_BIND 227 234 ATP. {ECO:0000256|HAMAP-Rule:MF_00983}. FT ZN_FING 446 458 C4-type. {ECO:0000256|HAMAP-Rule: FT MF_00983}. FT ZN_FING 473 489 C4-type. {ECO:0000256|HAMAP-Rule: FT MF_00983}. FT MOTIF 326 329 DEAH box. {ECO:0000256|HAMAP-Rule: FT MF_00983}. SQ SEQUENCE 738 AA; 81646 MW; AA466ADC5D8B8908 CRC64; MQAARILVDG QSDLVLDYGI PPEAGDVKPG CRVQVPLRNR TATGTVLTLS EPAPAWKDRL KPILKLIDPE PLISPVMMNL ASWAADYYSV ALDQMIRCLL PETVRQENTA EKMRKMVYLE KTPAREELDA LYRKAPRQAQ MLDYFSSAKQ QSAPLAAFGA GALNVARSLE AKGFISLKEE AVHRDPSTGE QFVPTQPMKL NSQQQKALEE ITAMCAAERK KPVLLQGVTG SGKTEVYLQA VSQIVKSGKS ALIMVPEISL TPQTVQRFKS RFAELPSSVA VLHSLLSDGE RFDEWHAIRS GKARIVIGPR SAVFAPLQNL GLVIVDEEHD ASYKQESSPR YHGRDLAVLR AHLENCAVLL GSATPSLESI HNALIGKYSL VKLTERADGQ QLPLIRILDM KTEGRNKSGP NVISERLRMS IDRRLDKGEQ VILLLNRRGF ARSIQCPDCG HVVTCLHCSL PLTYHRTEDR LMCHLCGFKA LPPRSCPECR SANILLQGYG TQKVEELLRR TFPAARITRV DADVARRKNA VRTILNQFRA HKIDILLGTQ MIAKGLDFPN VTLVGVLNAD LGLHIPDPRA GERTFQLLTQ VAGRAGRGDL SGEVIIQTFT PQSPSLQYAR HHDTDGFAAQ ELEMRRTFDL PPFTHIAVLT IRSQHESMAE FATQTLAARL RGMLPPPATM TDPMPAPIPR AHGQFRFQIT VKGPSARILS RTLRKLVQEA GLGEDLTAVI DVDAMSFM //