GenomeNet

Database: UniProt
Entry: M4S4T4_9SPHN
LinkDB: M4S4T4_9SPHN
Original site: M4S4T4_9SPHN 
ID   M4S4T4_9SPHN            Unreviewed;       480 AA.
AC   M4S4T4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   05-JUL-2017, entry version 33.
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   ECO:0000313|EMBL:AGH50786.1};
GN   ORFNames=G432_15340 {ECO:0000313|EMBL:AGH50786.1};
OS   Sphingomonas sp. MM-1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=745310 {ECO:0000313|EMBL:AGH50786.1, ECO:0000313|Proteomes:UP000011816};
RN   [1] {ECO:0000313|EMBL:AGH50786.1, ECO:0000313|Proteomes:UP000011816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MM-1 {ECO:0000313|EMBL:AGH50786.1};
RX   PubMed=23682148;
RA   Tabata M., Ohtsubo Y., Ohhata S., Tsuda M., Nagata Y.;
RT   "Complete Genome Sequence of the gamma-Hexachlorocyclohexane-Degrading
RT   Bacterium Sphingomonas sp. Strain MM-1.";
RL   Genome Announc. 1:E00247-13(2013).
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP004036; AGH50786.1; -; Genomic_DNA.
DR   EnsemblBacteria; AGH50786; AGH50786; G432_15340.
DR   KEGG; sphm:G432_15340; -.
DR   PATRIC; fig|745310.14.peg.3196; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000011816; 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; 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:UP000011816};
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:UP000011816}.
FT   DOMAIN      176    306       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      388    457       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     184    191       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   480 AA;  53262 MW;  F1BD8CEFBBEA807C CRC64;
     MTSAASFLST PDESGAGAID QAPSPFEAAW EAIRASLRKS CGARTFDGWL KPVTLVEFDS
     DEATVRLAAP SDFMANWVET HFAEQLLQAW RAMLPQVSKV AISADGGRPA LFTIPGDEAE
     AATQPEAEPP VAAPVAQAPV EHGFEARYSF DSFVVGKANE VAYNAARTVA EGGVLGFNPL
     FLHGGTGLGK THLMHAIGQE FLARQPGARI IYMSAEKFMY EFVAAMRAKD THSFKARLRA
     ADVLMIDDVQ FIAGKESTQE EFFHTMNEII SAGRRLVITA DRSPQDLEGI ESRILSRLSW
     GLVADVNPAD FELRLNIIVK KLEAMPQAKV PEDVVLFLAR RISTNVRELE GALNRVVAYS
     LLSGRPIDME FTQETLADML RATQRRITID EIQRRVCEHY RIKQSEMASS RRAREVARPR
     QIAMYLAKQL TPRSLPEIGR RFGGRDHTTV IHAVKQIEKL RQTDAELDAD VRLLMRQLEG
//
DBGET integrated database retrieval system