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Database: UniProt
Entry: Z5XMY1_9GAMM
LinkDB: Z5XMY1_9GAMM
Original site: Z5XMY1_9GAMM 
ID   Z5XMY1_9GAMM            Unreviewed;       462 AA.
AC   Z5XMY1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   25-OCT-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   ECO:0000313|EMBL:EWH04540.1};
GN   ORFNames=AT00_19035 {ECO:0000313|EMBL:EWH04540.1};
OS   Pseudoalteromonas lipolytica SCSIO 04301.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1452721 {ECO:0000313|EMBL:EWH04540.1, ECO:0000313|Proteomes:UP000021443};
RN   [1] {ECO:0000313|EMBL:EWH04540.1, ECO:0000313|Proteomes:UP000021443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 04301 {ECO:0000313|EMBL:EWH04540.1,
RC   ECO:0000313|Proteomes:UP000021443};
RA   Wang X., Tian X.;
RT   "Pseudoalteromonas lipolytica SCSIO 04301 Genome sequencing.";
RL   Submitted (FEB-2014) 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: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:EWH04540.1}.
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DR   EMBL; JDVB01000011; EWH04540.1; -; Genomic_DNA.
DR   RefSeq; WP_036973688.1; NZ_KK070036.1.
DR   EnsemblBacteria; EWH04540; EWH04540; AT00_19035.
DR   PATRIC; fig|1452721.3.peg.3667; -.
DR   Proteomes; UP000021443; 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: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:UP000021443};
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:UP000021443}.
FT   DOMAIN      159    361       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      370    439       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     167    174       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   462 AA;  52314 MW;  2DABF85B1F90F5E8 CRC64;
     MYLSVWQSCL YVLQDELPSQ QFSMWVRPLQ AESTEDTLTI YAPNRFVLDW VREKYLNRIN
     ELLVEICGDE APELRFDVGS KPILNAQAAV PAASAPVSAQ HTSEKQQPKP EKANVEPAPK
     SGYKSNIKEN YTFDSFVEGK SNQLAKAAAT QVADNPGSAF NPVFIYGGTG LGKTHLLHAV
     GNGIMANKPD AKIVYMHSER FVQDMVKALQ NNAIEEFKRY YRSVDALMID DIQFFANKER
     SQEEFFHTFN ALLEGNQQII LTSDRYPKEI EGVEDRLKSR FGWGLTIAIE PPELETRVAI
     LMKKAQQSKI NLPHEVAFFI AKKLRSNVRE LEGALNRVIA NANFTGRPIS IDFVKEALRD
     LLALQDKLVT IDNIQRTVAE YYRIRVSDLL SKRRSRSVAR PRQVAMALSK ELTNHSLPEI
     GDAFGGRDHT TVLHACRKVK SLRDESHEVK EDYQNLIRTL SS
//
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