GenomeNet

Database: UniProt
Entry: A0A142HBN9_9BACT
LinkDB: A0A142HBN9_9BACT
Original site: A0A142HBN9_9BACT 
ID   A0A142HBN9_9BACT        Unreviewed;       511 AA.
AC   A0A142HBN9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-SEP-2017, entry version 13.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=A0257_03760 {ECO:0000313|EMBL:AMR26297.1};
OS   Hymenobacter sp. PAMC 26554.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1484116 {ECO:0000313|EMBL:AMR26297.1, ECO:0000313|Proteomes:UP000075086};
RN   [1] {ECO:0000313|EMBL:AMR26297.1, ECO:0000313|Proteomes:UP000075086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 26554 {ECO:0000313|EMBL:AMR26297.1,
RC   ECO:0000313|Proteomes:UP000075086};
RA   Park H.;
RT   "Hymenobacter sp. genome sequencing.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in the initiation and regulation
CC       of chromosomal replication. Binds to the origin of replication; it
CC       binds specifically double-stranded DNA at a 9 bp consensus (dnaA
CC       box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic
CC       phospholipids. {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00756131}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP014771; AMR26297.1; -; Genomic_DNA.
DR   RefSeq; WP_068334353.1; NZ_CP014771.1.
DR   EnsemblBacteria; AMR26297; AMR26297; A0257_03760.
DR   KEGG; hyp:A0257_03760; -.
DR   KO; K02313; -.
DR   Proteomes; UP000075086; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 1.
DR   HAMAP; MF_00377; DnaA_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001957; Chromosome_initiator_DnaA.
DR   InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR   InterPro; IPR018312; Chromosome_initiator_DnaA_CS.
DR   InterPro; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR024633; DnaA_N_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF12; PTHR30050:SF12; 1.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   Pfam; PF08299; Bac_DnaA_C; 1.
DR   Pfam; PF11638; DnaA_N; 1.
DR   PRINTS; PR00051; DNAA.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00760; Bac_DnaA_C; 1.
DR   SUPFAM; SSF48295; SSF48295; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00362; DnaA; 1.
DR   PROSITE; PS01008; DNAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000075086};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075086}.
FT   DOMAIN      207    337       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      418    487       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     215    222       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   511 AA;  57366 MW;  5E809085004DAD43 CRC64;
     MSQDFRTVWA NCLRVIRAEV GEQSFRTWFE PVVPIELQGK VLTIQVPSVY FYEFLEEHYV
     EELKRAIYQE LGPEGRLEYS VVVDQGNAQA SAKTMHLPPA RKTAPSLAVP PEGRPHPNYG
     TAPGGIQPNR PVAQARHLVP GGNTATAAQV AANTLRNPFE AVKTMDRNIV PSQLNTTYTF
     DNYVEGDCNR LARSAGLAVA NKPGTTAFNP LMVYGGVGLG KTHLVQAIGN HIKATNTEKF
     VLYVSAEKFT NQFIESLQRN AVQDFANFYL LVDVLILDDV QFLANKGKTQ EMFFHIFNHL
     HQGGRQIVMT SDRPPRELSG LEDRLLSRFK WGLTADVQSP DFETRIAIIQ NKAQQDGMEI
     APQVVEYLAH SVPTNVRELE GVLTTLLAQS VLTRRDIDLE MAKGALRHII EEVEAEVNVD
     FIQKTVADYF SVPVALLKEK TRKKEIVTAR QVAMYFTKEH TNHSLKTIGY HFGGRDHATV
     IHSVQTVSDL IDSDRKFKEQ IGELRKKFVQ K
//
DBGET integrated database retrieval system