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Database: UniProt
Entry: M9YB35_AZOVI
LinkDB: M9YB35_AZOVI
Original site: M9YB35_AZOVI 
ID   M9YB35_AZOVI            Unreviewed;       478 AA.
AC   M9YB35;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|ARBA:ARBA00018893, ECO:0000256|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:AGK17774.1};
GN   ORFNames=AvCA6_00010 {ECO:0000313|EMBL:AGK17774.1};
OS   Azotobacter vinelandii CA6.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=1283331 {ECO:0000313|EMBL:AGK17774.1, ECO:0000313|Proteomes:UP000012988};
RN   [1] {ECO:0000313|EMBL:AGK17774.1, ECO:0000313|Proteomes:UP000012988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CA6 {ECO:0000313|EMBL:AGK17774.1,
RC   ECO:0000313|Proteomes:UP000012988};
RX   PubMed=23792740; DOI=10.1128/genomeA.00313-13;
RA   Noar J.D., Bruno-Barcena J.M.;
RT   "Complete Genome Sequences of Azotobacter vinelandii Wild-Type Strain CA
RT   and Tungsten-Tolerant Mutant Strain CA6.";
RL   Genome Announc. 1:E00313-E00313(2013).
CC   -!- FUNCTION: Plays an important role in the initiation and regulation of
CC       chromosomal replication. Binds to the origin of replication; it binds
CC       specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-
CC       TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
CC       {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00377}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|ARBA:ARBA00006583,
CC       ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU004227}.
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DR   EMBL; CP005095; AGK17774.1; -; Genomic_DNA.
DR   RefSeq; WP_012698697.1; NC_021150.1.
DR   AlphaFoldDB; M9YB35; -.
DR   SMR; M9YB35; -.
DR   KEGG; avd:AvCA6_00010; -.
DR   PATRIC; fig|1283331.3.peg.1; -.
DR   HOGENOM; CLU_026910_0_1_6; -.
DR   Proteomes; UP000012988; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; cd00009; AAA; 1.
DR   CDD; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.30.300.180; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00362; DnaA; 1.
DR   PANTHER; PTHR30050; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 1.
DR   PANTHER; PTHR30050:SF2; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48295; TrpR-like; 1.
DR   PROSITE; PS01008; DNAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00377};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00377};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00377};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00377};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00377}.
FT   DOMAIN          175..384
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          386..455
FT                   /note="Chromosomal replication initiator DnaA C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00760"
FT   BINDING         183..190
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   478 AA;  54007 MW;  6F54711ED849DD56 CRC64;
     MSVELWQQCV ELLRDELPAQ QFNTWIRPLQ VEADGDELRV YAPNRFVLDW VNEKYLGRLL
     ELLGERSEDV TPSVSLLIGS KRSSAPRAVQ PASPPPAVVQ AAPVAIEEAS AARTVDAQPV
     APATVRTERS VQVEGGLKHT SYLNRAFTFE NFVEGKSNQL ARAAAWQVAD NPKHGYNPLF
     LYGGVGLGKT HLMHAVGNHL LKKNPNAKVV YLHSERFVAD MVKALQLNAI NEFKRFYRSV
     DALLIDDIQF FAKKERSQEE FFHTFNALLE GGQQVILTSD RYPKEIEGLE ERLKSRFGWG
     LTVAVEPPEL ETRVAILMKK AEQTKVELPH DAAFFIAQRI RSNVRELEGA LKRVIAHSHF
     TNHPITIELI RESLKDLLAL QDKLVSIDNI QRTVAEYYKI KIADLLSKRR SRSVARPRQV
     AMALSKELTN HSLPEIGDSF GGRDHTTVLH ACRKIAELRE TDADIREDYK NLLRTLTT
//
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