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Database: UniProt
Entry: A0A162RIA1_9BACL
LinkDB: A0A162RIA1_9BACL
Original site: A0A162RIA1_9BACL 
ID   A0A162RIA1_9BACL        Unreviewed;       448 AA.
AC   A0A162RIA1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   23-MAY-2018, entry version 17.
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=PNBC_18935 {ECO:0000313|EMBL:OAB72057.1};
OS   Paenibacillus crassostreae.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1763538 {ECO:0000313|EMBL:OAB72057.1, ECO:0000313|Proteomes:UP000077134};
RN   [1] {ECO:0000313|EMBL:OAB72057.1, ECO:0000313|Proteomes:UP000077134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0068 {ECO:0000313|EMBL:OAB72057.1,
RC   ECO:0000313|Proteomes:UP000077134};
RA   Shin S.-K., Yi H.;
RT   "Paenibacillus sp. LPB0068, isolated from Crassostrea gigas.";
RL   Submitted (FEB-2016) 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:SAAS00747961}.
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:OAB72057.1}.
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DR   EMBL; LSFN01000036; OAB72057.1; -; Genomic_DNA.
DR   RefSeq; WP_068660897.1; NZ_LSFN01000036.1.
DR   EnsemblBacteria; OAB72057; OAB72057; PNBC_18935.
DR   KEGG; pcx:LPB68_11955; -.
DR   KO; K02313; -.
DR   Proteomes; UP000077134; 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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000077134};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00747973};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00748008};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077134}.
FT   DOMAIN      142    270       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      354    423       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     150    157       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   448 AA;  51114 MW;  6ACD6B80A21D9E19 CRC64;
     MESHTSELWQ QILSIIQSKL SKPSFDTWFK ATKATTMNEQ SIVISAPTTF AVEWLESRYT
     KLVGSTLFEV IGKQLEVKFV IEEAKIEDTI PTFTSSQPQI SHEESMTHML NPKYTFDTFV
     IGSGNRFAHA ASLAVAEAPA KAYNPLFLYG GVGLGKTHLM HAIGHYVLEH NPNSKVVYLS
     SEKFTNEFIN SIRDNRTESF RNKYRSVDIL LVDDIQFIAG KESTQEEFFH TFNALHEEVK
     QIIISSDRPP KEIPTLEERL RSRFEWGLIT DIQPPDLETR TAILRKKAKA ENLDIPNEAM
     MYIANQIDTN IRELEGALIR VVAYSSLTNQ DVTTHLAAEA LKDIIPSSRP KMITMQDIQQ
     KVGEYYNLRM DDFKARKRTK AIAFPRQIAM YLSRELTDYS LPKIGEAFGG RDHTTVIHAH
     EKISQLLKVD QDLFKVVNNL IEKIKNPT
//
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