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Database: UniProt
Entry: A0A1R1MIH4_9GAMM
LinkDB: A0A1R1MIH4_9GAMM
Original site: A0A1R1MIH4_9GAMM 
ID   A0A1R1MIH4_9GAMM        Unreviewed;       572 AA.
AC   A0A1R1MIH4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   16-JAN-2019, entry version 14.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=BGP75_01825 {ECO:0000313|EMBL:OMH39612.1};
OS   Motiliproteus sp. MSK22-1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Motiliproteus.
OX   NCBI_TaxID=1897630 {ECO:0000313|EMBL:OMH39612.1, ECO:0000313|Proteomes:UP000187359};
RN   [1] {ECO:0000313|EMBL:OMH39612.1, ECO:0000313|Proteomes:UP000187359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSK22-1 {ECO:0000313|EMBL:OMH39612.1,
RC   ECO:0000313|Proteomes:UP000187359};
RA   Nakajima Y., Yoshizawa S., Ogura Y., Hayashi T., Kogure K.;
RT   "Draft genome of Motiliproteus sp. strain MSK22-1.";
RL   Submitted (AUG-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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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:OMH39612.1}.
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DR   EMBL; MIEQ01000017; OMH39612.1; -; Genomic_DNA.
DR   RefSeq; WP_076714036.1; NZ_MIEQ01000017.1.
DR   Proteomes; UP000187359; 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   Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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   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:SAAS00756129};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000187359};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187359}.
FT   DOMAIN      269    474       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      480    549       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     277    284       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      431    451       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   572 AA;  63745 MW;  C34689BC68BAD116 CRC64;
     MPVDLWQKCL SYLQEEFPSQ QYNTWIRPLR AEAGSPSQLR LLAPNRFVMD WVSDKYLKRI
     KELLSEVDED RVYEVLLEVG ANGRRQGVGA ASAGRLSRQI QASDQFQNTD HSTVSVSSPG
     SSGHNSSASD TPGAATDIQG SSTANNSINK EPLYHGSSGS DSVSLGHSLD SSPLDQRSIS
     QNYSKTTSSE PGAPMQQDLL APQSTKPLQK KLKPGDGPNR KKRQVDVEGG VRHQTHLNKL
     FTFDTFVQGK SNQLGLAAAQ QVAENPGGSY NPLFIYGGVG LGKTHLMHAV GAAMLERNPN
     AKIVYLHSER FVADMVKALQ LNAINDFKRY YRSVDALLID DIQFFAGKDR SQEEFFHTFN
     ALLEGGQQMI LTCDRYPKEI SGLEDRLKSR FGWGLTVAIE PPELETRVAI LMKKAEEARI
     RLPHDAAFFI AQKIRSNVRE LEGALKRVIA NAHFTGSSIT TEFIRESLKD LLALQDKMIS
     IDNIQRVVAE YYKIKISDLH SKRRSRSVAR PRQVAMALSK ELTNHSLPEI GNSFGGRDHT
     TVLHARRKVA ELRESDTDIR EDYKNLLRLL SS
//
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