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Database: UniProt
Entry: F4KKS2_PORAD
LinkDB: F4KKS2_PORAD
Original site: F4KKS2_PORAD 
ID   F4KKS2_PORAD            Unreviewed;       475 AA.
AC   F4KKS2;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   25-OCT-2017, entry version 48.
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   OrderedLocusNames=Poras_0001 {ECO:0000313|EMBL:AEE11955.1};
OS   Porphyromonas asaccharolytica (strain ATCC 25260 / DSM 20707 / BCRC
OS   10618 / JCM 6326 / LMG 13178 / VPI 4198) (Bacteroides
OS   asaccharolyticus).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Porphyromonadaceae; Porphyromonas.
OX   NCBI_TaxID=879243 {ECO:0000313|EMBL:AEE11955.1, ECO:0000313|Proteomes:UP000006545};
RN   [1] {ECO:0000313|Proteomes:UP000006545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25260 / DSM 20707 / VPI 4198
RC   {ECO:0000313|Proteomes:UP000006545};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA   Pagani I., Lu M., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA   Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Porphyromonas asaccharolytica DSM 20707.";
RL   Submitted (APR-2011) 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:SAAS00911680}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
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DR   EMBL; CP002689; AEE11955.1; -; Genomic_DNA.
DR   RefSeq; WP_013759693.1; NC_015501.1.
DR   STRING; 879243.Poras_0001; -.
DR   EnsemblBacteria; AEE11955; AEE11955; Poras_0001.
DR   KEGG; pah:Poras_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000006545; 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:SF2; PTHR30050:SF2; 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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006545};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006545}.
FT   DOMAIN      173    307       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      384    453       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     181    188       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   475 AA;  53083 MW;  E4860023FC78BB54 CRC64;
     MTDREAALRA WSECTVLLQA MIQPEVYNAW FPHIKPVSLI GVEMTLGVPS QFFCEYIETH
     FINELKQVLQ RIVGPNVVLK YKALVDSAAS HRKNSSVTLP TQSYASNAYG AAGAYTINAN
     GAAAALKTEP RQLPDFDSQL KPQLSFDTYY QGESNRTASS IARSIAEKPG QGALNPCFIY
     GPSGVGKTHL CHAIGLRIRE LYPELKVLYV SSHMFEMQYV AATRANTTND FINFYQQVDV
     LLIDDIQGLI AKKKTQLTFF QVFNHLYMLG KQIVLTSDTA PVNLAGLEER LISRIAGSLT
     IEVERPDYDL RREYLRHKSE ESGSILPQEM IDYIARTVTS SIRGLQGVFF SLITRAAVEG
     CDVTSSFVKK IVSQTVKQEK KEITVSMIEK TVCEYYHVPI ELVRSRSRKA DVAQARQMIM
     YFAKRYTDQS LSAIGELLGG RSHATVLHSC KVVEDQAEVS TAYRSDLTAI ESLIK
//
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