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Database: UniProt
Entry: A0A0Q5VHK8_9ACTN
LinkDB: A0A0Q5VHK8_9ACTN
Original site: A0A0Q5VHK8_9ACTN 
ID   A0A0Q5VHK8_9ACTN        Unreviewed;       618 AA.
AC   A0A0Q5VHK8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-SEP-2017, entry version 16.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=ASG36_09430 {ECO:0000313|EMBL:KQS58309.1};
OS   Geodermatophilus sp. Leaf369.
OC   Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae;
OC   Geodermatophilus.
OX   NCBI_TaxID=1736354 {ECO:0000313|EMBL:KQS58309.1, ECO:0000313|Proteomes:UP000051830};
RN   [1] {ECO:0000313|EMBL:KQS58309.1, ECO:0000313|Proteomes:UP000051830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf369 {ECO:0000313|EMBL:KQS58309.1,
RC   ECO:0000313|Proteomes:UP000051830};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS58309.1, ECO:0000313|Proteomes:UP000051830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf369 {ECO:0000313|EMBL:KQS58309.1,
RC   ECO:0000313|Proteomes:UP000051830};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:SAAS00731907}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00756131}.
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:KQS58309.1}.
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DR   EMBL; LMQA01000002; KQS58309.1; -; Genomic_DNA.
DR   EnsemblBacteria; KQS58309; KQS58309; ASG36_09430.
DR   Proteomes; UP000051830; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF12; PTHR30050:SF12; 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; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000051830};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051830}.
FT   DOMAIN      310    438       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      522    591       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     318    325       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   618 AA;  69504 MW;  DA11492A8A4C18B8 CRC64;
     MPDPIDLATV WEGIRHRLAG SLTPQQTAML NLTRPLGLVE DVAVLAAPNE FTQTVLESRM
     RAALNEALSA EFGREIKVAV QLEDGPTPPP PREDREQAWP AEPARRPEWE RADRRDAEDR
     AREDRSRDER TRDDRNRDDR NREDRDRDDR DRDDEDRAAR AQLDDGRSAF GVRTDAPRRD
     AWLPESGDGR DWSRGTGYDR EAREDRAPAW DRPRADPRRP APWDQDDAAG DPGSATAGSE
     DGRPSDGDHG IGRDPGQAGA AGRGGYGDRR SPGSDLGLNP KYVFDSFVIG NSNRFAHAAA
     VAVAEAPARA YNPLFVYGDS GLGKTHLLHA IGHYAARMFP NVRVRYVSTE EFTNEFINLV
     HSGRAEDFRR RYRDIDFLLI DDIQFLERAE RTQEEFFHTF NTLHNASKQI VITSDRPPKK
     LTTLEDRLRT RFEWGLITDV QAPDLETRIA ILRKKAWGER LQAPDAVLEF IASKVQTNIR
     ELEGALIRVT AFASLNKQPV DLALAELVLK DLISDEQGPQ ITAAIIMAAT AEYFSVTMEE
     LQGANRSRTL VNARQIAMYL CRELTELSLP RIGASFGGKD HTTVMHAVKK ITGLMSERRA
     TYTQVTELTA RIKSRARQ
//
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