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Database: UniProt
Entry: R6HT30_9PROT
LinkDB: R6HT30_9PROT
Original site: R6HT30_9PROT 
ID   R6HT30_9PROT            Unreviewed;       483 AA.
AC   R6HT30;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-SEP-2017, entry version 29.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=BN570_00554 {ECO:0000313|EMBL:CDB40200.1};
OS   Azospirillum sp. CAG:260.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum; environmental samples.
OX   NCBI_TaxID=1262706 {ECO:0000313|EMBL:CDB40200.1, ECO:0000313|Proteomes:UP000018110};
RN   [1] {ECO:0000313|EMBL:CDB40200.1, ECO:0000313|Proteomes:UP000018110}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:260 {ECO:0000313|Proteomes:UP000018110};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-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:SAAS00724167}.
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:CDB40200.1}.
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DR   EMBL; CBDP010000055; CDB40200.1; -; Genomic_DNA.
DR   Proteomes; UP000018110; 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; IPR024633; DnaA_N_dom.
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   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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018110};
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:UP000018110}.
FT   DOMAIN      180    312       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      392    460       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     188    195       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   483 AA;  54900 MW;  694EF5ED1DAEF2FB CRC64;
     MAEEATTINN SVQDQWGQIC SQLKTEVGDT AFDSWLKPLT PGSFNDGVMN ICVPTRFMRN
     WVITHYSDRI HKIWEKKNPE IKSVNFVVQA VQDEAKGLYN PSCRSLLKKI SSSPSPSNIY
     QSGINSVLAN SNDFQAGNDS QQSLSVPLNP QYTFDNFVVG KTNEFAYAAA RKVAESRNVS
     FNPLFLYSGV GLGKTHLMHA IAWHIKQQDP TRNIVYLSAE KFMYKFVRAL RYKDTTAFKE
     QFRSVDVLMV DDVQFMGGKD TTQEEFFYTF NSLIEEGRQI IISADKSPAD LEGIETRLKS
     RLGCGLVADI HPTDFDLRIG ILENKARQLG IELPQKVAEF LAQKITSNIR ELEGALRRVI
     AHSQLLSDKE ITLDMTQDVL KDMLRSYDKR TTIDEIQKKV AEHFNISVKE MQSSRRARTV
     ARPRQIAMYL AKQLTSRSLP EIGRKFDRDH TTVMHAVRKV EELILEDASL AENVDALRRT
     LES
//
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