GenomeNet

Database: UniProt
Entry: A0A136PBS3_9BACT
LinkDB: A0A136PBS3_9BACT
Original site: A0A136PBS3_9BACT 
ID   A0A136PBS3_9BACT        Unreviewed;       441 AA.
AC   A0A136PBS3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   25-OCT-2017, entry version 12.
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   ORFNames=UZ07_CHB004001820 {ECO:0000313|EMBL:KXK55883.1};
OS   Chlorobi bacterium OLB7.
OC   Bacteria; Chlorobi.
OX   NCBI_TaxID=1619898 {ECO:0000313|EMBL:KXK55883.1, ECO:0000313|Proteomes:UP000070627};
RN   [1] {ECO:0000313|EMBL:KXK55883.1, ECO:0000313|Proteomes:UP000070627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB7 {ECO:0000313|EMBL:KXK55883.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) 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:SAAS00911680}.
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:KXK55883.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; LMYZ01000151; KXK55883.1; -; Genomic_DNA.
DR   PATRIC; fig|1619898.3.peg.2112; -.
DR   Proteomes; UP000070627; 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; IPR024633; DnaA_N_dom.
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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000070627};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070627}.
FT   DOMAIN      135    271       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   441 AA;  49425 MW;  435841E82DE2D0B3 CRC64;
     MQLDGATLTI EVPSQFFYEW IEEHYYALVR KTMVQVLGDQ AQLRYHTVVD NPNEPAEARF
     ITVPNRAAAA AGATVKYPAT QTGLPFSTPS IQQQAKPEST YLNSRFTFEN FVTGECNQLA
     YAAAKAVADN PGGTRFNPLV IYGGVGLGKT HLVQAIGHHV MQQRPGSSVV YISSERFTLE
     FVNAIQHNKS QEFINYYRNV DVLMVDDIQF FSDKEKTQDN FFHTFNALHH TGKQIVLTSD
     VPPKQLRGVD ERLISRFQWG LTTDIQPPDF ETRVAILQKM SISEGYDLPP DVIEYIARNV
     TSSVREMEGC LISLLAESSL RNLSLTLDLT REVVNGIAVT IDPVITIEQI QSAVCEHFNL
     PISLLTGKTR KQEIVQARQI AMALIRELTS TSLKTIGNHF GGRDHTTVMH AITMVDSLKD
     RDEPTRRALF AIRQKLNLPG Q
//
DBGET integrated database retrieval system