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Database: UniProt
Entry: L1MC66_9CORY
LinkDB: L1MC66_9CORY
Original site: L1MC66_9CORY 
ID   L1MC66_9CORY            Unreviewed;       508 AA.
AC   L1MC66;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   25-OCT-2017, entry version 36.
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=HMPREF9997_02220 {ECO:0000313|EMBL:EKX88546.1};
OS   Corynebacterium durum F0235.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1035195 {ECO:0000313|EMBL:EKX88546.1, ECO:0000313|Proteomes:UP000010445};
RN   [1] {ECO:0000313|EMBL:EKX88546.1, ECO:0000313|Proteomes:UP000010445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0235 {ECO:0000313|EMBL:EKX88546.1,
RC   ECO:0000313|Proteomes:UP000010445};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R.,
RA   Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M.,
RA   Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C.,
RA   Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S.,
RA   Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-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:SAAS00735475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00911680}.
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:EKX88546.1}.
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DR   EMBL; AMEM01000037; EKX88546.1; -; Genomic_DNA.
DR   EnsemblBacteria; EKX88546; EKX88546; HMPREF9997_02220.
DR   PATRIC; fig|1035195.3.peg.1987; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000010445; 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; 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:SF2; PTHR30050:SF2; 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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010445};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010445}.
FT   DOMAIN      200    328       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      413    482       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     208    215       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   508 AA;  56785 MW;  4A7553D9CF64D1EC CRC64;
     MRTKVAEHST SLEETWRQVV EDLLRLSEQP DSGIPTLNGR ARGFLKLVKP IALFNGFAVL
     STPHAMAKDA VEKDLGGYIT TVLSERMGRP YSLAVSIDPG VEEPDPEPPI VAATPEPAQA
     HPEGMWNTTS ISMPDQAATI SRGRFTHDDG RRFTREPAGP APQQDRSLNP RYTFENFVIG
     SSNRFAHAAA VAVAENPANA FNPLFISGGS GLGKTHLLHA AGNYAQVLQP GLRVKYVSSE
     EFTNDYINSV RDDRQESFKR RYRNLDILMV DDIQFLEGKE GTQEEFFHTF NALHQANKQI
     ILSSDRPPKQ LTTLEDRLRT RFEGGLITDI QPPDLETRIA ILEKKAQIDQ TVMDRDVLEL
     IASRFEASIR ELEGALIRVS AYSSLNGETT ISREMAEIAL RDIMPEAPDV EITASTIMEV
     TADYFDVSLD ALRGSGKTRA VAYARQLAMY LCRELTDLSL PKIGDNFGGK DHTTVMYADR
     KIRKEMTEKR DTYNQIQELT QIIKNRGR
//
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