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Database: UniProt
Entry: U2IVP8_9PORP
LinkDB: U2IVP8_9PORP
Original site: U2IVP8_9PORP 
ID   U2IVP8_9PORP            Unreviewed;       467 AA.
AC   U2IVP8;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
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   ORFNames=HMPREF1556_01053 {ECO:0000313|EMBL:ERJ71877.1};
OS   Porphyromonas sp. oral taxon 278 str. W7784.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=1227272 {ECO:0000313|EMBL:ERJ71877.1, ECO:0000313|Proteomes:UP000016628};
RN   [1] {ECO:0000313|EMBL:ERJ71877.1, ECO:0000313|Proteomes:UP000016628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W7784 {ECO:0000313|EMBL:ERJ71877.1,
RC   ECO:0000313|Proteomes:UP000016628};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in the initiation and regulation of
CC       chromosomal replication. Binds to the origin of replication; it binds
CC       specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-
CC       TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
CC       {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00377}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|ARBA:ARBA00006583,
CC       ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU004227}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERJ71877.1}.
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DR   EMBL; AWUX01000065; ERJ71877.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2IVP8; -.
DR   STRING; 1227272.HMPREF1556_01053; -.
DR   PATRIC; fig|1227272.3.peg.862; -.
DR   eggNOG; COG0593; Bacteria.
DR   HOGENOM; CLU_026910_3_0_10; -.
DR   Proteomes; UP000016628; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; cd00009; AAA; 1.
DR   CDD; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.30.300.180; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR038454; DnaA_N_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   NCBIfam; TIGR00362; DnaA; 1.
DR   PANTHER; PTHR30050; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 1.
DR   PANTHER; PTHR30050:SF2; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48295; TrpR-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00377};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00377};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00377};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00377};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00377}.
FT   DOMAIN          161..294
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          375..444
FT                   /note="Chromosomal replication initiator DnaA C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00760"
FT   BINDING         169..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   467 AA;  52885 MW;  32B5C0E726A0DCBA CRC64;
     MLLAHDYARH TLMHTPIPQD GEQLWKHCLQ IIARSCDPQT LQRWFAPIRP LGVETREDEG
     GSFEALVLEV PSKSFYEELL RTHETLLIRA QQEVLTPRGL EIFLAPAQVA PAPSPAKIAR
     TQDYTSHLSA DLRFETFYES ACNREALRIA EATAARPGQA PLNFIFIYGP SGVGKTHLCQ
     AIGQRAMELH PTMRVCYVSS SKFETQFIRD SLMRGTERGM FIDFYQQMDI LIIDDIQGLI
     GKTKTQQAFF DIFNHLYLLG KQIIVTCDVP PVDLKGMEAR IMTRIQSAMM LRIDRPDLEL
     RRKILQRRVA DSGVELGEEC VEFIAENMQD NVRQLEGAIR TIVTHSKFSD LGAVDIDMTR
     RIVGGTVSIE RKEVTPELVL DTVCKVFGVE KDQLRTPSRK AVLALPRQVT MYLVKKHTSA
     SYNTIAQLLN RSDHTTIMHG CKAIEGRINI EPALKERIAL VEEELRG
//
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