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Database: UniProt
Entry: A0A126T4G1_9GAMM
LinkDB: A0A126T4G1_9GAMM
Original site: A0A126T4G1_9GAMM 
ID   A0A126T4G1_9GAMM        Unreviewed;       438 AA.
AC   A0A126T4G1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   16-JAN-2019, entry version 20.
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   ECO:0000313|EMBL:AMK76952.1};
GN   ORFNames=JT25_010710 {ECO:0000313|EMBL:AMK76952.1};
OS   Methylomonas denitrificans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomonas.
OX   NCBI_TaxID=1538553 {ECO:0000313|EMBL:AMK76952.1, ECO:0000313|Proteomes:UP000030512};
RN   [1] {ECO:0000313|EMBL:AMK76952.1, ECO:0000313|Proteomes:UP000030512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJG1 {ECO:0000313|EMBL:AMK76952.1,
RC   ECO:0000313|Proteomes:UP000030512};
RX   PubMed=25580993; DOI=10.1111/1462-2920.12772;
RA   Kits K.D., Klotz M.G., Stein L.Y.;
RT   "Methane oxidation coupled to nitrate reduction under hypoxia by the
RT   Gammaproteobacterium Methylomonas denitrificans, sp. nov. type strain
RT   FJG1.";
RL   Environ. Microbiol. 17:3219-3232(2015).
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}.
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DR   EMBL; CP014476; AMK76952.1; -; Genomic_DNA.
DR   RefSeq; WP_036276157.1; NZ_CP014476.1.
DR   EnsemblBacteria; AMK76952; AMK76952; JT25_010710.
DR   KEGG; mdn:JT25_010710; -.
DR   KO; K02313; -.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000030512; Chromosome.
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   Complete proteome {ECO:0000313|Proteomes:UP000030512};
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:UP000030512}.
FT   DOMAIN      135    266       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      346    415       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     143    150       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   438 AA;  49594 MW;  A0D451095417D03F CRC64;
     MSVIWNNCLA KLEHEIPSTD FSTWIRPLQA VETDSQLKLL APNRFIIDHI KQHFFAVIED
     AVNEFSNATL AVQFEIGSKK SPAIKAPILS KSPTQKKNQP NFLNKAFTFE SFVEGKSNQL
     ARAASVTVSD NIGKVYNPLF IYGSSGLGKT HLMHAIGNAV LLKKPDANIV YLHSEKFVQD
     MVKALQQNSI NQFKEYYRSI DILLMDDIQF LAGKERSQEE FFHTFNNLLD NKHQVVLTCD
     KYPKEIDGLE DRLKSRFGWG LPVAIEPPDL ETRAAILIKK AMQVGVDLDQ DIAFFIAKRI
     PSNVRDLEGA LRRVVANSQF TGRDITLEFT KEALHDLISL QDKLISIDNI QKTVAEYFKI
     RVADLSSKNR KQSITRPRQV AMCLARELTS HSYPEIGDAF GGRDHTTVIN ACKRVAELKD
     DDVKMAEDYK NLLRTLSH
//
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