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Database: UniProt
Entry: A0A0G3H9N4_9CORY
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ID   A0A0G3H9N4_9CORY        Unreviewed;       551 AA.
AC   A0A0G3H9N4;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
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:AKK10034.1};
GN   ORFNames=CUTER_00005 {ECO:0000313|EMBL:AKK10034.1};
OS   Corynebacterium uterequi.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1072256 {ECO:0000313|EMBL:AKK10034.1, ECO:0000313|Proteomes:UP000035548};
RN   [1] {ECO:0000313|EMBL:AKK10034.1, ECO:0000313|Proteomes:UP000035548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45634 {ECO:0000313|EMBL:AKK10034.1,
RC   ECO:0000313|Proteomes:UP000035548};
RX   PubMed=26227590;
RA   Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT   "Virulence Factor Genes Detected in the Complete Genome Sequence of
RT   Corynebacterium uterequi DSM 45634, Isolated from the Uterus of a Maiden
RT   Mare.";
RL   Genome Announc. 3:e00783-15(2015).
RN   [2] {ECO:0000313|Proteomes:UP000035548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45634 {ECO:0000313|Proteomes:UP000035548};
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete genome sequence of Corynebacterium uterequi DSM 45634, isolated
RT   from the uterus of a maiden mare.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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; CP011546; AKK10034.1; -; Genomic_DNA.
DR   RefSeq; WP_047258706.1; NZ_CP011546.1.
DR   AlphaFoldDB; A0A0G3H9N4; -.
DR   STRING; 1072256.CUTER_00005; -.
DR   KEGG; cut:CUTER_00005; -.
DR   PATRIC; fig|1072256.5.peg.1; -.
DR   OrthoDB; 9807019at2; -.
DR   Proteomes; UP000035548; 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; 3.40.50.300; 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; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000035548}.
FT   DOMAIN          244..372
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          456..525
FT                   /note="Chromosomal replication initiator DnaA C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00760"
FT   REGION          91..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..161
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         252..259
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   551 AA;  61667 MW;  12DD62B0FE6AEA24 CRC64;
     MTDHSIDYTT TWNEVVAEIL TQANRPESSI PTLNYAQQVF LKLASPMLIV DGYMVLSVPD
     NHAKSVIENE LSAHITSVMA QRTGQPCTLA VTTSRADSTP APAQPAQTAH TVQAPHPAPP
     AAPNSRPASP RPTDPSPQPA PRGRTPQPIE DPIPPRGPYQ PGEQLPMNLE ELAEQHRNQQ
     EQRRRTAHPT APAPQRIPRE KPAHDPNRET SLNPKYTFES FVIGSSNRFA NGAAVAVAEA
     PARAYNPLFI WGGSGLGKTH LLHAAGNYAK ELQPGLRVKY VSSEEFTNDY INSVRDDRQE
     AFKRRYRNLD ILMVDDIQFL EGKEGTQEEF FHTFNALHQA DKQIILSSDR PPKELTTLED
     RLRTRFEGGL ITDIQPPDLE TRIAILEKKA AADGNQVDRR VLEMIASHFD TSVRELEGNL
     LRVTAYASLA NLPVTVEVAE VALRDLLSGD DNVEITPALI KEAVADYFHL DIDTLIGKGR
     KRQEVHPRQL AMYLCRELTE LSLPKIGQEF GGRDHTTVMY SHTKITQEMT ENHETYDEVH
     HLTQMIKNHR R
//
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