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Database: UniProt
Entry: E7RZL9_9BURK
LinkDB: E7RZL9_9BURK
Original site: E7RZL9_9BURK 
ID   E7RZL9_9BURK            Unreviewed;       592 AA.
AC   E7RZL9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   13-FEB-2019, entry version 51.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:EFV94013.1};
GN   ORFNames=HMPREF0551_2128 {ECO:0000313|EMBL:EFV94013.1};
OS   Lautropia mirabilis ATCC 51599.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Lautropia.
OX   NCBI_TaxID=887898 {ECO:0000313|EMBL:EFV94013.1, ECO:0000313|Proteomes:UP000011021};
RN   [1] {ECO:0000313|EMBL:EFV94013.1, ECO:0000313|Proteomes:UP000011021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51599 {ECO:0000313|EMBL:EFV94013.1,
RC   ECO:0000313|Proteomes:UP000011021};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z.,
RA   Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L.,
RA   Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D.,
RA   Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R.,
RA   San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S.,
RA   Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K.,
RA   Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (DEC-2010) 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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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:EFV94013.1}.
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DR   EMBL; AEQP01000022; EFV94013.1; -; Genomic_DNA.
DR   RefSeq; WP_005674520.1; NZ_GL636062.1.
DR   STRING; 887898.HMPREF0551_2128; -.
DR   EnsemblBacteria; EFV94013; EFV94013; HMPREF0551_2128.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; 219876at2; -.
DR   BioCyc; GCF_000186425-HMP:HMPREF0551_RS10300-MONOMER; -.
DR   Proteomes; UP000011021; 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   Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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   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:SAAS00756129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000011021};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011021}.
FT   DOMAIN      287    421       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      498    567       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     295    302       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   592 AA;  64328 MW;  74441F9B6562029F CRC64;
     MQEQWDACSA AIAARMPEQA YKTWIKPLAF LEFSADDCLI RLGAATQIKA DIVRNQYQNL
     IQEVLRDVID PAMRVEIGVA PRAASAAPVA GAGAGAATHA GPSSFASAGP THPGSMSHGV
     QPPAPHGGGQ GNVPAGMGNV AAGAGSYQGG MASPHGAGAF QPQAHVPQQT HERPGHGPGY
     GGSQGWSDGG AEHAGHPGFE ARHALEAPDV LDDGTGDYLD DGSDPEGPGD DGSTNAPARS
     FGGLGGQMPN ERSRLNPGLT FAAFVNGKAN DLARAAALQV ADRPGSAYNP LFIHGGVGLG
     KTHLMQAVGN AIQQRESRAI IRYISSNQFV QDLIQAIRRN AIDRFKHYYQ SLDVLLIDDI
     QFLSDKQRSQ EEFFHVFETM TINQRQIVIT CDTYPKELKG IDDRLISRLN SGLIVAIEPP
     ELEMRVAILQ RKAEQARIRL PDDVAYFIAK NIRRNVRELE GALQRAIHYA SFRSSPLTLE
     LVKEALKDLI SFNRGQISID FIQKTVAEYY KIKQADMYSK RKPAKIALPR QIAMYLAKEL
     TQKSLPEIGD AFGGKDHTTV LYAVRKITEL RAHDEDLNKQ IHVLDQTLRE YL
//
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