GenomeNet

Database: UniProt
Entry: A0A0R2PZP3_9ACTN
LinkDB: A0A0R2PZP3_9ACTN
Original site: A0A0R2PZP3_9ACTN 
ID   A0A0R2PZP3_9ACTN        Unreviewed;       456 AA.
AC   A0A0R2PZP3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-SEP-2017, entry version 12.
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=ABR67_06835 {ECO:0000313|EMBL:KRO43332.1};
OS   Acidimicrobium sp. BACL17 MAG-120823-bin42.
OC   Bacteria; Actinobacteria; Acidimicrobiia; Acidimicrobiales;
OC   Acidimicrobiaceae; Acidimicrobium.
OX   NCBI_TaxID=1655575 {ECO:0000313|EMBL:KRO43332.1, ECO:0000313|Proteomes:UP000051003};
RN   [1] {ECO:0000313|EMBL:KRO43332.1, ECO:0000313|Proteomes:UP000051003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL27 MAG-120823-bin42 {ECO:0000313|EMBL:KRO43332.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C.,
RA   Pinhassi J., Andersson A.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-2015) 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:KRO43332.1}.
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; LIAZ01000073; KRO43332.1; -; Genomic_DNA.
DR   Proteomes; UP000051003; Unassembled WGS sequence.
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: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.
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:UP000051003};
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:UP000051003}.
FT   DOMAIN      151    279       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      363    432       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     159    166       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   456 AA;  51742 MW;  10F7215C58F8C9B8 CRC64;
     MLRAQVSEAV WFSTFNDAVA VADDKMSLRL QVPNTYVRER ILTRYMSLVR DALDEVGASE
     RQLLIDVQTN TADDVHEQLA NNNTPDVLPA ELNHTISPSH TSSSTTSKSR NGKGTAVGLN
     PRYTFETFVK GTSNQFALAA AQRVAETPGR SYNPLFIYGS AGLGKTHLLH AIGYYVHQNY
     AHYEVRYVST ETFLNEYVDG IRSNTIAAFK RRYREVDVLL IDDIQFMEGK EGLQEEFFHT
     FNSLHGANKQ IVISSDRMPD AIPTLEDRLR GRFRWGLITD IQPPDMETRL AILRNKAERD
     RTSVSHEVLE FIANNVTTNI RELEGALIRV GAYSSLNKTQ VDVALAKQLL TDLLTRTAIK
     PRTDEQLLVE IAEHLGFEVD ALRGKSRQRP LVQARQTAMY VFRELTDLSY PAIARLFGDR
     DHTTVIHAVD KTQRMMSERK QVYEQVTELV QKFKTS
//
DBGET integrated database retrieval system