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Database: UniProt
Entry: A0A1C7PFN0_9BACT
LinkDB: A0A1C7PFN0_9BACT
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ID   A0A1C7PFN0_9BACT        Unreviewed;       477 AA.
AC   A0A1C7PFN0;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Replicative DNA helicase {ECO:0000256|ARBA:ARBA00021957, ECO:0000256|RuleBase:RU362085};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|RuleBase:RU362085};
GN   ORFNames=PYTT_1465 {ECO:0000313|EMBL:SEH88748.1};
OS   Akkermansia glycaniphila.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC   Akkermansiaceae; Akkermansia.
OX   NCBI_TaxID=1679444 {ECO:0000313|EMBL:SEH88748.1, ECO:0000313|Proteomes:UP000176204};
RN   [1] {ECO:0000313|Proteomes:UP000176204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Koehorst J.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Participates in initiation and elongation during chromosome
CC       replication; it exhibits DNA-dependent ATPase activity.
CC       {ECO:0000256|RuleBase:RU362085}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665,
CC         ECO:0000256|RuleBase:RU362085};
CC   -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC       {ECO:0000256|ARBA:ARBA00008428, ECO:0000256|RuleBase:RU362085}.
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DR   EMBL; LT629973; SEH88748.1; -; Genomic_DNA.
DR   RefSeq; WP_067771978.1; NZ_LT629973.1.
DR   AlphaFoldDB; A0A1C7PFN0; -.
DR   STRING; 1679444.PYTT_1465; -.
DR   KEGG; agl:PYTT_1465; -.
DR   PATRIC; fig|1679444.3.peg.1467; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000176204; Chromosome i.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-UniRule.
DR   CDD; cd00984; DnaB_C; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR   InterPro; IPR007692; DNA_helicase_DnaB.
DR   InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR   InterPro; IPR007693; DNA_helicase_DnaB-like_N.
DR   InterPro; IPR016136; DNA_helicase_N/primase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00665; DnaB; 1.
DR   PANTHER; PTHR30153:SF2; REPLICATIVE DNA HELICASE; 1.
DR   PANTHER; PTHR30153; REPLICATIVE DNA HELICASE DNAB; 1.
DR   Pfam; PF00772; DnaB; 1.
DR   Pfam; PF03796; DnaB_C; 1.
DR   SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51199; SF4_HELICASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362085};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU362085};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362085};
KW   Helicase {ECO:0000256|RuleBase:RU362085, ECO:0000313|EMBL:SEH88748.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362085};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362085}; Primosome {ECO:0000256|RuleBase:RU362085};
KW   Reference proteome {ECO:0000313|Proteomes:UP000176204}.
FT   DOMAIN          197..473
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  53155 MW;  80104E7F50092C81 CRC64;
     MSNDATSFSP LELTKAPASS PESRTVPQAP RVEKSVLSMM TIDPSYILGR CITKGMGEEY
     FYVPAHKLLW NIFLDRYNKN QPLDITSVAQ ELTDKHQLEA VGGLAGLTEI YSYTTNTALF
     DPHFETLQEK YVLRSIIATT SRSMEKAFAA EEEIAELLDS VEQDVLGIRE KMKHGEEQSL
     STVIAEAVTN MERFLAQKGG ILGITTGFEK LDRMSNGLKA GELFVVAARP SMGKTSFLLN
     MMEHIALDLN KPSLIFSCEM PSVQLVERLI FARSGIRRAE MMARGSMTQQ EQKHFARVVS
     VLRKSRLVLD DTAAISINEL RAKARRVLRD QGELAAIGID YLQLMRSHTK QAQNSREREI
     AEISSGLKSL AKELKVPIIV LAQLNRGPEN RTGGSLGVPR MSDLRESGAI EQDADMIGLL
     YRSAYYAEND EERQQRAGHA NLLLAKNRNG PTGDVPLYFE AELMRFSTRQ DEEGSGE
//
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