GenomeNet

Database: UniProt
Entry: E2PVR8_STRC2
LinkDB: E2PVR8_STRC2
Original site: E2PVR8_STRC2 
ID   E2PVR8_STRC2            Unreviewed;       597 AA.
AC   E2PVR8;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   05-JUL-2017, entry version 46.
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   ECO:0000313|EMBL:EFG07982.1};
GN   ORFNames=SCLAV_2911 {ECO:0000313|EMBL:EFG07982.1};
OS   Streptomyces clavuligerus (strain ATCC 27064 / DSM 738 / JCM 4710 /
OS   NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=443255 {ECO:0000313|EMBL:EFG07982.1, ECO:0000313|Proteomes:UP000002357};
RN   [1] {ECO:0000313|EMBL:EFG07982.1, ECO:0000313|Proteomes:UP000002357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 /
RC   NRRL 3585 / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357};
RX   PubMed=20624727; DOI=10.1093/gbe/evq013;
RA   Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA   Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C.,
RA   Bovenberg R.A.L., Breitling R., Takano E.;
RT   "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT   evolutionary reservoir of secondary metabolic pathways.";
RL   Genome Biol. Evol. 2:212-224(2010).
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:SAAS00731907}.
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; CM000913; EFG07982.1; -; Genomic_DNA.
DR   ProteinModelPortal; E2PVR8; -.
DR   STRING; 443255.SCLAV_2911; -.
DR   EnsemblBacteria; EFG07982; EFG07982; SCLAV_2911.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   Proteomes; UP000002357; Chromosome.
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; 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   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:UP000002357};
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:UP000002357}.
FT   DOMAIN      290    418       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      504    573       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     298    305       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   597 AA;  66100 MW;  DC5D8234DAA78F6F CRC64;
     MADVPADLAA VWPRVLEHLL AEGRAGIEPK DKQWIERCRP LALVAGTALL SVPNEWGKRV
     LEGRLAPLIS ETLSRECGGP IRIAITVDDS AAGAPAPQET APQPSAYPQH DEAPGYPPQP
     DPYGGYGHRA ADEGLPEIRP VYPEYQQQRP EPGAWPRAQE DLSWQQPRLG GFPERDAYQE
     RETFQDRDPY ATARPDRTPH DYRSPQPPAE RPGYEQRPDR RELPAPAAPH RGTGGTGPGP
     LGSPSPAASG PGEPHARLNP KYLFDTFVIG ASNRFAHAAA VAVAEAPAKA YNPLFIYGES
     GLGKTHLLHA IGHYARSLYP GTRVRYVSSE EFTNEFINSI RDGKGDAFRK RYRDVDILLV
     DDIQFLASKE STQEEFFHTF NTLHNANKQI VLSSDRPPKQ LMTLEDRLRN RFEWGLTTDV
     QPPELETRIA ILRKKAVQEQ LNAPPEVLEF IASRISRNIR ELEGALIRVT AFASLNRQPV
     DLGLTEIVLK DLIPGGEDSA PEITAGAIMA ATADYFGLTV EDLCGSSRSR VLVTARQIAM
     YLCRELTDLS LPKIGAQFGG RDHTTVMHAD RKIRALMAER RSIYNQVTEL TNRIKNG
//
DBGET integrated database retrieval system