GenomeNet

Database: UniProt
Entry: C7REZ5_ANAPD
LinkDB: C7REZ5_ANAPD
Original site: C7REZ5_ANAPD 
ID   C7REZ5_ANAPD            Unreviewed;       459 AA.
AC   C7REZ5;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   25-OCT-2017, entry version 66.
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   OrderedLocusNames=Apre_0001 {ECO:0000313|EMBL:ACV28056.1};
OS   Anaerococcus prevotii (strain ATCC 9321 / DSM 20548 / JCM 6508 / PC1)
OS   (Peptostreptococcus prevotii) (Peptococcus prevotii).
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Anaerococcus.
OX   NCBI_TaxID=525919 {ECO:0000313|EMBL:ACV28056.1, ECO:0000313|Proteomes:UP000002294};
RN   [1] {ECO:0000313|EMBL:ACV28056.1, ECO:0000313|Proteomes:UP000002294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9321 / DSM 20548 / JCM 6508 / PC1
RC   {ECO:0000313|Proteomes:UP000002294};
RX   PubMed=21304652; DOI=10.4056/sigs.24194;
RA   Labutti K., Pukall R., Steenblock K., Glavina Del Rio T., Tice H.,
RA   Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chain P., Saunders E., Brettin T., Detter J.C., Han C.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Anaerococcus prevotii type strain
RT   (PC1).";
RL   Stand. Genomic Sci. 1:159-165(2009).
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001708; ACV28056.1; -; Genomic_DNA.
DR   RefSeq; WP_012803475.1; NC_013171.1.
DR   ProteinModelPortal; C7REZ5; -.
DR   STRING; 525919.Apre_0001; -.
DR   EnsemblBacteria; ACV28056; ACV28056; Apre_0001.
DR   KEGG; apr:Apre_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000002294; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002294};
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      156    287       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      368    436       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     164    171       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      436    459       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   459 AA;  52809 MW;  27809593C717F15D CRC64;
     MTNLEYITDE LKNEMKMHVT DTQQFDTWIS ILKPLNLYSE TLYLEVPKKD TLFIYDKIWV
     PQLQLALDNI KDKTGKDLKV SVIAKDSDDY NKVLTLGKDY DPNGQMRISK VNSFPRPQLE
     EENIFANFVE GKSNQYALGV SQAVAENISN KSQARLYNPL FIYGESGLGK THLMQAIAHE
     ILDNRDDAYV MYLSSEKFTN EMISALRSTK NEKFREKYRS VDILLIDDIQ FIAGKEGTQE
     EFFHTFNDLY NTGKQIVISS DRPPKEIKHL ENRLISRFSW GIIVDIGKPD FETRVAILQK
     KLDQLGAYID NNILFYIAEN IDTNIRDLEG ALSTAIAYAK SDNREVVTME DAIKGVATRV
     KDKKKHVGID DIQKYVADKY GIKLSDIKGK SRKKEIVNPR QIAMFLSREI LEDSLVTISN
     AFDRDHTTVM HGIDKIQKQI EEDDNFKEEI DTLLKEITE
//
DBGET integrated database retrieval system