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Database: UniProt
Entry: K1DUD8_9MICO
LinkDB: K1DUD8_9MICO
Original site: K1DUD8_9MICO 
ID   K1DUD8_9MICO            Unreviewed;       621 AA.
AC   K1DUD8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=B277_15078 {ECO:0000313|EMBL:EKA60029.1}, CWN80_06190
GN   {ECO:0000313|EMBL:RWU83989.1};
OS   Janibacter hoylei PVAS-1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=1210046 {ECO:0000313|EMBL:EKA60029.1, ECO:0000313|Proteomes:UP000004474};
RN   [1] {ECO:0000313|EMBL:RWU83989.1, ECO:0000313|Proteomes:UP000288711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PVAS-1 {ECO:0000313|EMBL:RWU83989.1,
RC   ECO:0000313|Proteomes:UP000288711};
RX   PubMed=19643890; DOI=10.1099/ijs.0.002527-0;
RA   Shivaji S., Chaturvedi P., Begum Z., Pindi P.K., Manorama R.,
RA   Padmanaban D.A., Shouche Y.S., Pawar S., Vaishampayan P., Dutt C.B.,
RA   Datta G.N., Manchanda R.K., Rao U.R., Bhargava P.M., Narlikar J.V.;
RT   "Janibacter hoylei sp. nov., Bacillus isronensis sp. nov. and Bacillus
RT   aryabhattai sp. nov., isolated from cryotubes used for collecting air from
RT   the upper atmosphere.";
RL   Int. J. Syst. Evol. Microbiol. 59:2977-2986(2009).
RN   [2] {ECO:0000313|EMBL:EKA60029.1, ECO:0000313|Proteomes:UP000004474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PVAS-1 {ECO:0000313|EMBL:EKA60029.1,
RC   ECO:0000313|Proteomes:UP000004474};
RX   PubMed=23144385; DOI=10.1128/JB.01728-12;
RA   Pawar S.P., Dhotre D.P., Shetty S.A., Chowdhury S.P., Chaudhari B.L.,
RA   Shouche Y.S.;
RT   "Genome Sequence of Janibacter hoylei MTCC8307, Isolated from the
RT   Stratospheric Air.";
RL   J. Bacteriol. 194:6629-6630(2012).
RN   [3] {ECO:0000313|EMBL:RWU83989.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PVAS-1 {ECO:0000313|EMBL:RWU83989.1};
RA   Seuylemezian A., Cooper K., Vaishampayan P.;
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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:EKA60029.1}.
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DR   EMBL; ALWX01000084; EKA60029.1; -; Genomic_DNA.
DR   EMBL; PIPF01000006; RWU83989.1; -; Genomic_DNA.
DR   RefSeq; WP_007929571.1; NZ_PIPF01000006.1.
DR   AlphaFoldDB; K1DUD8; -.
DR   STRING; 1210046.B277_15078; -.
DR   PATRIC; fig|1210046.3.peg.2898; -.
DR   eggNOG; COG0515; Bacteria.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000004474; Unassembled WGS sequence.
DR   Proteomes; UP000288711; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06577; PASTA_pknB; 3.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF6; SERINE/THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF03793; PASTA; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:EKA60029.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:EKA60029.1};
KW   Transferase {ECO:0000313|EMBL:EKA60029.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..285
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          364..429
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          430..497
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          499..560
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          308..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..621
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   621 AA;  65785 MW;  156CB0592B2C8B6E CRC64;
     MSAAAPRLLG GRYEVGELIG RGGMAEVHLG HDTRLGRPVA IKILRTDHAR DAAFLGRFRR
     EAQSVAGLNH RSIVAVYDSG EDRVVEAGGA HLDIPYIVME YVDGRTLREL LNESETGTLE
     PTEAARIVQQ VLEALDYSHD MGIVHRDIKP GNVMIADDGA VKVMDFGIAR AIADTQATMT
     QTQAVIGTAQ YISPEQARGE TVDKRSDVYS TGCLLFELLT GRTPYTGEPI SLTYQHVNAD
     IPLPSSVNPQ VPPQLDAIVH HALTKDRDER YPDAKSMAED LEAYRGGRPI SPVATERLDA
     ATTALPVVAP RGEPTPRTDP ETASMPVAQQ RRRGGGLGWL MAALLLIPIA LLGWFAWDAS
     QGEEVVQVTV PKVVGSDEDA AVAKLESVGL KADVETVTDD GAVGTVIAQD PGEGTSVPEG
     DTVVIQVSGG PDEVGVPSVV GMGRNEATKA LQDAGLEVGE ITEEDSPDQG PNRVISSSPG
     PAESVAKGSK VDLVIASGDV DLQDYTGQKI DDVRSDLFGL KLKIKETTRE SDEDEGTILE
     QSPGEGKIRQ GRTVTFVVAR KPAETVTTTP SSSETSDEPS DSESSEPNPT STSPSAPLTP
     TPSEPSSTRS TSSTTQSPAS P
//
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