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Database: UniProt
Entry: C0XTI0_9CORY
LinkDB: C0XTI0_9CORY
Original site: C0XTI0_9CORY 
ID   C0XTI0_9CORY            Unreviewed;       534 AA.
AC   C0XTI0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-SEP-2017, entry version 57.
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:EEI16477.1};
GN   ORFNames=HMPREF0298_1750 {ECO:0000313|EMBL:EEI16477.1};
OS   Corynebacterium lipophiloflavum DSM 44291.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=525263 {ECO:0000313|EMBL:EEI16477.1, ECO:0000313|Proteomes:UP000006196};
RN   [1] {ECO:0000313|EMBL:EEI16477.1, ECO:0000313|Proteomes:UP000006196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44291 {ECO:0000313|EMBL:EEI16477.1,
RC   ECO:0000313|Proteomes:UP000006196};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C.,
RA   Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L.,
RA   Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y.,
RA   Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L.,
RA   Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F.,
RA   Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M.,
RA   Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S.,
RA   Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J.,
RA   Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J.,
RA   Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D.,
RA   Worley K., Gibbs R.;
RL   Submitted (JAN-2009) 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:EEI16477.1}.
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DR   EMBL; ACHJ01000141; EEI16477.1; -; Genomic_DNA.
DR   RefSeq; WP_006839040.1; NZ_GG667191.1.
DR   ProteinModelPortal; C0XTI0; -.
DR   STRING; 525263.HMPREF0298_1750; -.
DR   EnsemblBacteria; EEI16477; EEI16477; HMPREF0298_1750.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000006196; 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:UP000006196};
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:UP000006196}.
FT   DOMAIN      225    353       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      437    506       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     233    240       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   534 AA;  59268 MW;  10B88907D72CA525 CRC64;
     MVDQQLAALW RDIVSELLTL SERPNSNVPT LTHQERAYLQ LVTPVMLVDG YVILAAPHAA
     AKTVIENSLG THITALLSRK LNTTCTLAVS IQQPEPVANE QPRPLDSKPE QTSVPDWFST
     SSRPPAFTED ATPGEVGEQI PMGLDELARL HSQHQAEAKG ASGGRRQASA HPTVPQRLPR
     ETPAHNPDRE ASLNPKYTFE NFVIGSSNRF ANGAAVAVAE NPARAYNPLF IWGGSGLGKT
     HLLHAAGNYA KLLQPNLRIS YVSSEEFTND YINSVRDDRQ ESFKRRYRNL DILMVDDIQF
     LEGKEGTQEE FFHTFNALHQ QNKQIILSSD RPPRQLTTLE DRLRTRFEGG LITDVQPPDL
     ETRIAILMKK AAADGTHVDH AVLELIASQF ESSIRELEGA LIRVSAYSSL INEPITLEVA
     QVALRDLLPN GGEVTISAAV IKEAAAEYFD ISLDQLTGAG KTRLVAHARQ LAMYLCRELT
     DLSLPKIGDE FGGKDHTTVM YADRKIRKEM TENRGTYDEI QVLTQMIKNQ ARSR
//
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