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Database: UniProt
Entry: A4AEW1_9ACTN
LinkDB: A4AEW1_9ACTN
Original site: A4AEW1_9ACTN 
ID   A4AEW1_9ACTN            Unreviewed;       471 AA.
AC   A4AEW1;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   05-JUL-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   ORFNames=A20C1_09784 {ECO:0000313|EMBL:EAR26162.1};
OS   marine actinobacterium PHSC20C1.
OC   Bacteria; Actinobacteria.
OX   NCBI_TaxID=312284 {ECO:0000313|EMBL:EAR26162.1, ECO:0000313|Proteomes:UP000003868};
RN   [1] {ECO:0000313|EMBL:EAR26162.1, ECO:0000313|Proteomes:UP000003868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHSC20C1 {ECO:0000313|EMBL:EAR26162.1,
RC   ECO:0000313|Proteomes:UP000003868};
RA   Murray A., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (FEB-2006) 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: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   -!- 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:EAR26162.1}.
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DR   EMBL; AAOB01000001; EAR26162.1; -; Genomic_DNA.
DR   RefSeq; WP_009773594.1; NZ_CH672415.1.
DR   ProteinModelPortal; A4AEW1; -.
DR   STRING; 312284.A20C1_09784; -.
DR   EnsemblBacteria; EAR26162; EAR26162; A20C1_09784.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000003868; 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; 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:UP000003868};
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:UP000003868}.
FT   DOMAIN      160    288       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      372    441       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     168    175       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   471 AA;  53018 MW;  39532AC6DC0BF0A8 CRC64;
     MSETPDPTKG LWQTVLAHLD GDERITPQLQ GFVSLVEPKG VMAGTLYLEV PNELTRGMLE
     QRLRQPLLDA IGSLSGEHGI NNFATVVNPD IQQDALSQEI PRAEQPYIEP TPPTPIEQSP
     PRRSDSRLNP KYSFDNFVIG GSNRFAHAAA VAVAEAPAKA YNPLFIYGGS GLGKTHLLHA
     IGHYAESLYP GIRVRYVSSE EFTNDFINSI ANNRASVFQS RYREIDILLI DDIQFLQGKD
     STQEAFFHTF NTLHDHNKQV VITSDLPPKH LTGFEDRMRS RFEWGLITDV QAPDLETRIA
     ILRKKAQSEK MQVGNDILEF MASKVSSNIR ELEGTLIRVT AFASLNRTEV DMALVQTVLK
     DLITLDEDNV IAPVDIINHT ADYFKLTVDD LYGSSRSQAV ATARQIAMYL CREMTNLSLP
     KIGQLFGNRD HTTVMYANKK ITELMKERRS IYNQVTELTS RIKQNHRFSK N
//
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