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Database: UniProt
Entry: A0A151AK87_9CLOT
LinkDB: A0A151AK87_9CLOT
Original site: A0A151AK87_9CLOT 
ID   A0A151AK87_9CLOT        Unreviewed;       455 AA.
AC   A0A151AK87;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-SEP-2017, entry version 12.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:KYH28031.1};
GN   ORFNames=CLCOL_23010 {ECO:0000313|EMBL:KYH28031.1};
OS   Clostridium colicanis DSM 13634.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121305 {ECO:0000313|EMBL:KYH28031.1, ECO:0000313|Proteomes:UP000075374};
RN   [1] {ECO:0000313|EMBL:KYH28031.1, ECO:0000313|Proteomes:UP000075374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13634 {ECO:0000313|EMBL:KYH28031.1,
RC   ECO:0000313|Proteomes:UP000075374};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium colicanis DSM 13634.";
RL   Submitted (FEB-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:SAAS00724167}.
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:KYH28031.1}.
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DR   EMBL; LTBB01000014; KYH28031.1; -; Genomic_DNA.
DR   RefSeq; WP_061859099.1; NZ_LTBB01000014.1.
DR   EnsemblBacteria; KYH28031; KYH28031; CLCOL_23010.
DR   PATRIC; fig|1121305.3.peg.2304; -.
DR   Proteomes; UP000075374; 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; IPR024633; DnaA_N_dom.
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   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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000075374};
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:UP000075374}.
FT   DOMAIN      150    278       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      362    431       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     158    165       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   455 AA;  51850 MW;  733826D9B12DFDAF CRC64;
     MDAQLNQLWD KTLNIIKGEL TEVSFNTWIK SIVPISLEQN TIKLQVPNDF TRGILESRYK
     DLIVNAIKLI TSKKYNIDFL ISSEDKLSDD KTSINNTSKS SKAKKSNIIV SDEMSSMLNP
     KYTFDSFVIG NSNRFAHAAS LAVAEAPAKA YNPLFIYGGV GLGKTHLMHA IGHYILQNNP
     KAKVVYVSSE KFTNELINSI KDDKNEEFRN KYRNVDVLLI DDSQFIAGKE RTQEEFFHTF
     NTLYEADKQI ILSSDRPPKE IPTLEDRLRS RFEWGLIADI QAPDFETRIA ILKKKADVEK
     LNIPNDVMVY IATKIKSNIR ELEGALIRTV AYSSLTNREI SVELAAEALK DIISNEENKQ
     VTIDLIQDVV SNYFNLKIED LKSSRRTRNI AFPRQIAMYL SRKLTDMSLP KIGEEFGGRD
     HTTVIHAYEK ISTNLKNDES LRNVINDLTK KINNN
//
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