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Database: UniProt
Entry: B6AQG6_9BACT
LinkDB: B6AQG6_9BACT
Original site: B6AQG6_9BACT 
ID   B6AQG6_9BACT            Unreviewed;       660 AA.
AC   B6AQG6;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Probable lipopolysaccharide biosynthesis protein {ECO:0000313|EMBL:EDZ38487.1};
GN   ORFNames=CGL2_10954040 {ECO:0000313|EMBL:EDZ38487.1};
OS   Leptospirillum sp. Group II '5-way CG'.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=419541 {ECO:0000313|EMBL:EDZ38487.1};
RN   [1] {ECO:0000313|EMBL:EDZ38487.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14961025; DOI=10.1038/nature02340;
RA   Tyson G.W., Chapman J., Hugenholtz P., Allen E.E., Ram R.J.,
RA   Richardson P.M., Solovyev V.V., Rubin E.M., Rokhsar D.S., Banfield J.F.;
RT   "Community structure and metabolism through reconstruction of microbial
RT   genomes from the environment.";
RL   Nature 428:37-43(2004).
RN   [2] {ECO:0000313|EMBL:EDZ38487.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18651792; DOI=10.1371/journal.pbio.0060177;
RA   Simmons S.L., Dibartolo G., Denef V.J., Goltsman D.S., Thelen M.P.,
RA   Banfield J.F.;
RT   "Population genomic analysis of strain variation in Leptospirillum group II
RT   bacteria involved in acid mine drainage formation.";
RL   PLoS Biol. 6:E177-E177(2008).
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DR   EMBL; DS995261; EDZ38487.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6AQG6; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd05387; BY-kinase; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   PANTHER; PTHR32309; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR32309:SF13; TYROSINE-PROTEIN KINASE ETK-RELATED; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        22..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        358..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          632..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..652
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   660 AA;  73723 MW;  B9AE404917C07CDD CRC64;
     MQTLDAKTII ALAWLSLRRH KLIAVVTFFL LLIPVSIVGL MKKPVYVAKA TVLIKQNNYA
     SSSLANHLHT PRSLGIQLAI LKSQYLAGKV IDNLPERTIK DLEENAEYTD YQSKFINVIR
     TTLGKSPIIM NPREKAAMEL RNARMGFRGA GYGGIIEISG ESTDPHVALD LVNGYIDSFK
     DISSHFALEQ QADLDKSLSL QILNARSLLK KSEEDLLDFQ NRAEKRGGKH HRVDVSSYLS
     QESDMLSALR MRKAQLLLTE TRSHPDVVAV TQEIREIEKK VGKLHSIAKP GDGSMGVSGS
     AWESFLESNI KMDKDLLSEL EQERSSARII ADSNLENLIV IDPPLLPVKP QMTKGFKIIL
     VGVAGALGGA VAVPFLLVFF RKPIQGETNL KKLSGVPNFA NIPRLSSRHI PERNGVRVPR
     IDQMADKESA WIFEKEFESM FFRLKKTLKL QKGQVLLITS PAPEDGKSVT SLNLALTMAR
     MGHHTTLMDA DTIRGRVQQN LRSVNHFQAE EFLPGNDEGP RVIDWNQGNL AVITLEKSPT
     RFWMEHPEPV LAKWFEILRF QSDFILIDSP PILASTDLLG ISSLVDGVLI VARNNVTQER
     DFLRVESVLK EHHFEIMGTV LNDSTSPHIQ YSYGYTPESK KKPRDSSKTS SKTKKKGISG
//
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