GenomeNet

Database: UniProt
Entry: A0A139TP71_9BACT
LinkDB: A0A139TP71_9BACT
Original site: A0A139TP71_9BACT 
ID   A0A139TP71_9BACT        Unreviewed;       447 AA.
AC   A0A139TP71;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   25-OCT-2017, entry version 13.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=HMPREF3039_02214 {ECO:0000313|EMBL:KXU53493.1};
OS   Akkermansia sp. KLE1798.
OC   Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales;
OC   Akkermansiaceae; Akkermansia.
OX   NCBI_TaxID=1574265 {ECO:0000313|EMBL:KXU53493.1, ECO:0000313|Proteomes:UP000070454};
RN   [1] {ECO:0000313|EMBL:KXU53493.1, ECO:0000313|Proteomes:UP000070454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLE1798 {ECO:0000313|EMBL:KXU53493.1,
RC   ECO:0000313|Proteomes:UP000070454};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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:SAAS00747914}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00911680}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KXU53493.1}.
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; LTZM01000048; KXU53493.1; -; Genomic_DNA.
DR   EnsemblBacteria; KXU53493; KXU53493; HMPREF3039_02214.
DR   PATRIC; fig|1574265.3.peg.2155; -.
DR   Proteomes; UP000070454; Unassembled WGS sequence.
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; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF2; PTHR30050:SF2; 1.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   Pfam; PF08299; Bac_DnaA_C; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000070454};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895}.
FT   DOMAIN      140    267       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      355    424       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     148    155       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   447 AA;  50029 MW;  3494368EB40A1642 CRC64;
     MSPEVYGLWF PKFSLLEDSG KTLTLVCDDP MAALWVENSY TPELKQAAML ALGGERNVKF
     ICADEVASEQ ETDAPAQKSS VRKKNAQPEE SPARTAKKAR PQGARAALND LYTFDSFVMY
     EDSRFAYQAA ISAAQSERPL FNPLFLYGKS GVGKTHLLQA IGHEVLRQES SANVVYVTGE
     QFANEFIDAS RTQNGQSFAK LRRKYRKADV LLVDDVQFIS GKEKTVEEFL HTFDALFHAH
     KTIVLCADAA ACDISNLDVR LAARLESGLT VELTLPGDED RLEILRSKRD RAGMNVSDEI
     LEFLASRIQK SVRRLEGALL RVATFTSLSG DMPDISKIEQ LLRDILREET SRVLSVETIQ
     KRVADFYELK VSDLTGKRRP NSIAFPRQIA MYLSRRLTEC SLKDIGNAFG GRDHGTVIHA
     NKLVASRMEN DVRVRDIVLR LEEDLQG
//
DBGET integrated database retrieval system