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Database: UniProt
Entry: I0GWT4_ACTM4
LinkDB: I0GWT4_ACTM4
Original site: I0GWT4_ACTM4 
ID   I0GWT4_ACTM4            Unreviewed;       593 AA.
AC   I0GWT4;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   05-JUL-2017, entry version 44.
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:BAL85221.1};
GN   OrderedLocusNames=AMIS_10 {ECO:0000313|EMBL:BAL85221.1};
OS   Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64
OS   / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Actinoplanes.
OX   NCBI_TaxID=512565 {ECO:0000313|EMBL:BAL85221.1, ECO:0000313|Proteomes:UP000007882};
RN   [1] {ECO:0000313|EMBL:BAL85221.1, ECO:0000313|Proteomes:UP000007882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 /
RC   NBRC 102363 / 431 {ECO:0000313|Proteomes:UP000007882};
RA   Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H.,
RA   Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.;
RT   "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC
RT   102363).";
RL   Submitted (FEB-2012) 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}.
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DR   EMBL; AP012319; BAL85221.1; -; Genomic_DNA.
DR   EnsemblBacteria; BAL85221; BAL85221; AMIS_10.
DR   KEGG; ams:AMIS_10; -.
DR   PATRIC; fig|512565.3.peg.1; -.
DR   KO; K02313; -.
DR   OMA; VADGQET; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000007882; 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:UP000007882};
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:UP000007882}.
FT   DOMAIN      287    415       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      499    568       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     295    302       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   593 AA;  66128 MW;  D17A35FF4DA01DD7 CRC64;
     MADQVDLGEV WKATLGELSD EIASPQQRAY LQLVRLRAIV EDTALLSVPD AFTRDVIESR
     MRGAITEVLT RRLSRPIQVA VTVRPPEDGS GIPGTVYGTP IDAAPTPLEP QPRHYADPPR
     YDDQPRYDDA GPYQPELPGY PGQQRSPEPY PTGSAQHSRT VPAARDGQET LFADPMPPQL
     PQPPMNRPPT RPVEKAAEPQ APDDSALPRA TPDAAQRRPE MMPPTRGDNG PGRPPVDLRG
     PGASPRPGGN DGNRLNPKYM FETFVIGSSN RFAHAAAVAV AESPAKAYNP LFIYGSSGLG
     KTHLLHAIGH YATTLGHARS VRYVSTEEFT NDFINSLRDD KTQAFQRRYR DVDILLIDDI
     QFLENRERTQ EEFFHTFNTL HNANKQIVIS SDRSPRQLAT LEDRMRTRFE WGLLADIQPP
     DLETRIAILQ KKAAQERMYA PDDVLEFIAS RVSSSIRELE GALIRVTAFA SLTRSPVQLS
     LAEEVLRDFM PDGAGPEITA DQIMVSTADY FGVSLEDLRG HSRSRVLVNA RQVAMYLCRE
     LTDLSLPRIG QAFGGRDHTT VMHADRKIRQ HMAERRSLYN QIAELTNRIK QNT
//
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