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Database: UniProt
Entry: A0A0Q1AJK7_9CORY
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Original site: A0A0Q1AJK7_9CORY 
ID   A0A0Q1AJK7_9CORY        Unreviewed;       532 AA.
AC   A0A0Q1AJK7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-2017, entry version 17.
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   ECO:0000313|EMBL:KQB87032.1};
GN   ORFNames=Clow_00077 {ECO:0000313|EMBL:KQB87032.1};
OS   Corynebacterium lowii.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1544413 {ECO:0000313|EMBL:KQB87032.1, ECO:0000313|Proteomes:UP000050488};
RN   [1] {ECO:0000313|EMBL:KQB87032.1, ECO:0000313|Proteomes:UP000050488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML 130206 {ECO:0000313|EMBL:KQB87032.1,
RC   ECO:0000313|Proteomes:UP000050488};
RA   Bernard K., Pacheco A.L., Mcdougall C., Burtx T., Weibe D., Tyler S.,
RA   Olson A.B., Cnockaert M., Eguchi H., Kuwahara T., Nakayama-Imaohji H.,
RA   Boudewijins M., Van Hoecke F., Bernier A.-M., Vandamme P.;
RT   "Corynebacteirum lowii and Corynebacterium oculi species nova, derived
RT   from human clinical disease and and emended description of
RT   Corynebacterium mastiditis.";
RL   Submitted (OCT-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:SAAS00735475}.
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:KQB87032.1}.
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DR   EMBL; LKEV01000001; KQB87032.1; -; Genomic_DNA.
DR   RefSeq; WP_055174754.1; NZ_LKEV01000001.1.
DR   EnsemblBacteria; KQB87032; KQB87032; Clow_00077.
DR   PATRIC; fig|1544413.3.peg.80; -.
DR   Proteomes; UP000050488; 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:SF2; PTHR30050:SF2; 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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000050488};
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:UP000050488}.
FT   DOMAIN      223    351       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      435    504       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     231    238       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   532 AA;  59324 MW;  855B65336B550379 CRC64;
     MTDDAAALQR TWHEVMRDLL YQANLPDSAI PTLTARQQAF LKLAQPITIV QGYVLLAVPH
     KMAKDVVEDE LGGYITQVFS QRMNQPCGLA VSVDPQKAGA ASKEAPLEPT PEPTPTTPPH
     AEQTAEQTKP PAASESSSPY YRSSEEWQTS HAPAQPPLRP KQTVVEEPQA STAQRLPREK
     PAHDPNRENS LNAKYTFESF VIGSSNRFAN SAAVAVAENP ARAYNPLFIS GGSGLGKTHL
     LHAAGNYAKL LQPTLRIKYV SSEEFTNDYI NSVRDDRQES FKRRYRNLDI LMVDDIQFLQ
     GKEGTQEEFF HTFNALHQAE KQIILSSDRP PKELTTLEDR LRTRFQAGLI ADIQPPDLET
     RIAILMKKAQ ADGTQVDRSV LELIASRFES SIRELEGALI RVSAYSSLIN EPIDMQTAEI
     ALRDILPEAS DVEITPTTII EVTAEYFGIT TDALCGVGKT RAVSHARQLA MYLCRELTDL
     SLPRIGAQFG GKDHTTVMYA ERKIRKEMQE KQDTYDEIHQ LTQIIKSRGR SI
//
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