GenomeNet

Database: UniProt
Entry: A0A0N8PSP2_9CHLR
LinkDB: A0A0N8PSP2_9CHLR
Original site: A0A0N8PSP2_9CHLR 
ID   A0A0N8PSP2_9CHLR        Unreviewed;       504 AA.
AC   A0A0N8PSP2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   05-JUL-2017, entry version 12.
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=SE17_10555 {ECO:0000313|EMBL:KPV53277.1};
OS   Kouleothrix aurantiaca.
OC   Bacteria; Chloroflexi; Kouleothrix.
OX   NCBI_TaxID=186479 {ECO:0000313|EMBL:KPV53277.1, ECO:0000313|Proteomes:UP000050509};
RN   [1] {ECO:0000313|EMBL:KPV53277.1, ECO:0000313|Proteomes:UP000050509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COM-B {ECO:0000313|EMBL:KPV53277.1,
RC   ECO:0000313|Proteomes:UP000050509};
RA   Hemp J.;
RT   "Draft genome sequence of Kouleothrix aurantiaca JCM 19913.";
RL   Submitted (SEP-2015) 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   -!- 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:KPV53277.1}.
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; LJCR01000295; KPV53277.1; -; Genomic_DNA.
DR   EnsemblBacteria; KPV53277; KPV53277; SE17_10555.
DR   PATRIC; fig|186479.3.peg.6108; -.
DR   Proteomes; UP000050509; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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:UP000050509};
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:UP000050509}.
FT   DOMAIN      197    325       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      409    478       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     205    212       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   504 AA;  56195 MW;  2FB151BD12244C3A CRC64;
     MNLAKVWNST LGTMQIQISR HEFNTWLRRA TLISLENGVA TIGAPSAFFK EGLENRYIGP
     LRELIGNLVG FPVQVRVIIA PPAPVAAEHR LASREYGKDD DMPDLDESPG YAAANAQQGY
     VPANGYANGA SNGSGMHNGN GNGNGYDRLN MQQLEFSSAM RSGMLNARYT FDRFIVGSSN
     RLANAACMAV AEHPAHAYNP LFLYGGVGLG KTHLLHAIGN YALDRDPEIN VLYVSSEKFT
     NDLINAIRRQ QTEEFRIRYR NIDILLIDDI QFIAGKESTQ EEFFHTFNTL HSAGKQIVIS
     SDRPPKAILT LEERLRSRFE WGLIVDVQTP DLETRTAILR AKAEQMSTHI PAEVIDFLAH
     RIQSNIRELE GCLNRVAAYA QLIGAPVSTE VATAALNELL DTTRRKRVTT EAILREVAEF
     YGVDLRAMQG RGRSRNIVVP RQVAMYLLRV ETDSSLMDIG QMLGGRDHTT VIYGCEKIGE
     EINSDSRLRQ EVVTIRDRLY QRAA
//
DBGET integrated database retrieval system