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
//