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Database: UniProt
Entry: A0A0X1RX61_9BACL
LinkDB: A0A0X1RX61_9BACL
Original site: A0A0X1RX61_9BACL 
ID   A0A0X1RX61_9BACL        Unreviewed;       447 AA.
AC   A0A0X1RX61;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-SEP-2017, entry version 14.
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   ECO:0000313|EMBL:AMA63109.1};
GN   ORFNames=ASO14_2897 {ECO:0000313|EMBL:AMA63109.1};
OS   Kurthia sp. 11kri321.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX   NCBI_TaxID=1750719 {ECO:0000313|EMBL:AMA63109.1, ECO:0000313|Proteomes:UP000058129};
RN   [1] {ECO:0000313|EMBL:AMA63109.1, ECO:0000313|Proteomes:UP000058129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11kri321 {ECO:0000313|EMBL:AMA63109.1,
RC   ECO:0000313|Proteomes:UP000058129};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-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: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}.
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DR   EMBL; CP013217; AMA63109.1; -; Genomic_DNA.
DR   RefSeq; WP_068456863.1; NZ_CP013217.1.
DR   EnsemblBacteria; AMA63109; AMA63109; ASO14_2897.
DR   KEGG; kur:ASO14_2897; -.
DR   PATRIC; fig|1750719.3.peg.2832; -.
DR   KO; K02313; -.
DR   Proteomes; UP000058129; Chromosome.
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:UP000058129};
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:UP000058129}.
FT   DOMAIN      143    272       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      355    424       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     151    158       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   447 AA;  50374 MW;  F182C93F2BA900CF CRC64;
     MNQEELKHFW SQVLHEAKKI ISKPSFDTWL KSTELIAYED DQLVVSAENS FSKEWLAKNY
     VTTIQGIVKK LTGSSLDIHF TEVADDDFQP STKRKKKELP VVANDHSPAM LNTKNTFDTF
     VIGPGNRFAH AASLAVAEAP AKAYNPLFLH GGVGLGKTHL MHAIGHYVLE HDPNAKVVYL
     SSEKFTNEFI NSIRDNNTEA FRNKYRKVDV LLIDDIQFLA GKESTQEEFF HTFNTLHEES
     KQIIISSDRQ PKEIPTLEDR LRSRFEWGLI IDIGPPDLET RIAILRKKAD ADGLQISDDV
     MSYIASQIDS NIRELEGALT RVVAYSNLLN QPLTAELAAE ALKSIMPSTT PKILSILDIQ
     KTVGEHYGIK LEDFSAKKRT KSIAFPRQVA MYLSREMTDS SLPKIGEEFG GRDHTTVIHA
     HEKITSLLKT DAILQDDIKQ IKTKLSN
//
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