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Database: UniProt
Entry: A0A1S1MNX4_9GAMM
LinkDB: A0A1S1MNX4_9GAMM
Original site: A0A1S1MNX4_9GAMM 
ID   A0A1S1MNX4_9GAMM        Unreviewed;       466 AA.
AC   A0A1S1MNX4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   16-JAN-2019, entry version 15.
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:OHU86421.1};
GN   ORFNames=BET10_01585 {ECO:0000313|EMBL:OHU86421.1};
OS   Pseudoalteromonas amylolytica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1859457 {ECO:0000313|EMBL:OHU86421.1, ECO:0000313|Proteomes:UP000179786};
RN   [1] {ECO:0000313|EMBL:OHU86421.1, ECO:0000313|Proteomes:UP000179786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JW1 {ECO:0000313|EMBL:OHU86421.1,
RC   ECO:0000313|Proteomes:UP000179786};
RA   Wu Y.-H., Cheng H., Jin X.-B., Wang C.-S., Xu X.-W.;
RT   "Pseudoalteromonas amylolytica sp. nov., isolated from the surface
RT   seawater.";
RL   Submitted (SEP-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: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:OHU86421.1}.
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DR   EMBL; MKJU01000038; OHU86421.1; -; Genomic_DNA.
DR   RefSeq; WP_070988039.1; NZ_MKJU01000038.1.
DR   Proteomes; UP000179786; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000179786};
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:UP000179786}.
FT   DOMAIN      163    365       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      374    443       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     171    178       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      325    345       {ECO:0000256|SAM:Coils}.
FT   COILED      443    463       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   466 AA;  52566 MW;  2B17C9D7A926A78E CRC64;
     MYLSVWQSCL YVLQDELPSQ QFSMWVRPLQ AESTEDTLTI YAPNRFVLDW VREKYLNRIN
     ELLIEICGNE APELRFDVGS KPIMGGVSVE DKQPSANAAS SGSELAPSAP IASSNTQKVE
     PAPKSAYKPN IKENYTFDNF VEGKSNQLAK AAATQVADNP GSAFNPVFIY GGTGLGKTHL
     LHAVGNGILD KKPDAKIVYM HSERFVQDMV KALQNNAIEE FKRYYRSVDA LMIDDIQFFA
     NKERSQEEFF HTFNALLEGN QQIILTSDRY PKEIEGVEDR LKSRFGWGLT IAIEPPELET
     RVAILMKKAQ QSNISLPHEV AFFIAKKLRS NVRELEGALN RVIANANFTG RPISIDFVKE
     ALRDLLALQD KLVTIDNIQR TVAEYYRIRV SDLLSKRRSR SVARPRQVAM ALSKELTNHS
     LPEIGDAFGG RDHTTVLHAC RKVKALRDES HEVKEDYQNL IRTLSS
//
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