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Database: UniProt
Entry: G4CSU3_9NEIS
LinkDB: G4CSU3_9NEIS
Original site: G4CSU3_9NEIS 
ID   G4CSU3_9NEIS            Unreviewed;       517 AA.
AC   G4CSU3;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   05-JUL-2017, entry version 37.
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:EGZ44558.1};
GN   ORFNames=HMPREF9370_2084 {ECO:0000313|EMBL:EGZ44558.1};
OS   Neisseria wadsworthii 9715.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=1030841 {ECO:0000313|EMBL:EGZ44558.1, ECO:0000313|Proteomes:UP000005336};
RN   [1] {ECO:0000313|EMBL:EGZ44558.1, ECO:0000313|Proteomes:UP000005336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9715 {ECO:0000313|EMBL:EGZ44558.1,
RC   ECO:0000313|Proteomes:UP000005336};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z.,
RA   Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L.,
RA   Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D.,
RA   Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R.,
RA   San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S.,
RA   Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K.,
RA   Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JUN-2011) 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:EGZ44558.1}.
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DR   EMBL; AGAZ01000070; EGZ44558.1; -; Genomic_DNA.
DR   RefSeq; WP_009117224.1; NZ_JH165159.1.
DR   EnsemblBacteria; EGZ44558; EGZ44558; HMPREF9370_2084.
DR   PATRIC; fig|1030841.3.peg.2075; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000005336; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005336};
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:UP000005336}.
FT   DOMAIN      214    344       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      425    494       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     222    229       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      376    403       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   517 AA;  58651 MW;  A8A4E4CEF5FE6F8A CRC64;
     MTLAEFWPLC LDRLHDTLTP QQFDTWIAPL TVGEENGQWV IYGKNQFSVN MLKKQFFQSI
     ERVRAEIAPE SPTLLFKTGK GQSFTRAGQA VSSDIQSCLS EITGKPKTSP LPSQKSLSEN
     TSEPQTTQKN TAKASAAEIL AERIKNLPTT SKKVKTEEPK KTQVKIEAEK EKAEQFYAQT
     NLSHDYTFDT LVEGKGNRIA AAAAQSIVEN PGKSYNPFFL YGSTGLGKTH LVQAIGNELL
     KNKPNAKVRY MHSDDYIRSF MNAVRSNSYE TFKQQYKQYD LLIIDDIQFI KGKERTMEEF
     FYLYNHFHNE KKQLILTCDV LPTKIEDMDD RLKSRFSWGL TLELEPPELE MRVAILQKKA
     ETAGVELDEQ AAFFIAKHIR SNVRELEGAF KRVEARSRFL KKKIDIDLAA EALQDIVASA
     YKIITADLIM DTVAKHYRIK ISDLLGAKRT RNIARPRQVA MSLTKELTNL SLPAIGDAFG
     GRDHTTVMHA VKTVAKLRNE DPELAQDYEK LLILIQN
//
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