ID I7ZBU7_9GAMM Unreviewed; 822 AA.
AC I7ZBU7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-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=WQQ_29410 {ECO:0000313|EMBL:EIT69359.1};
OS Hydrocarboniphaga effusa AP103.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Hydrocarboniphaga.
OX NCBI_TaxID=1172194 {ECO:0000313|EMBL:EIT69359.1, ECO:0000313|Proteomes:UP000003704};
RN [1] {ECO:0000313|EMBL:EIT69359.1, ECO:0000313|Proteomes:UP000003704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP103 {ECO:0000313|EMBL:EIT69359.1,
RC ECO:0000313|Proteomes:UP000003704};
RX PubMed=22933753; DOI=10.1128/JB.01017-12;
RA Chang H.K., Zylstra G.J., Chae J.C.;
RT "Genome Sequence of n-Alkane-Degrading Hydrocarboniphaga effusa Strain
RT AP103T (ATCC BAA-332T).";
RL J. Bacteriol. 194:5120-5120(2012).
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:EIT69359.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKGD01000002; EIT69359.1; -; Genomic_DNA.
DR RefSeq; WP_007185882.1; NZ_AKGD01000002.1.
DR AlphaFoldDB; I7ZBU7; -.
DR STRING; 1172194.WQQ_29410; -.
DR PATRIC; fig|1172194.4.peg.2849; -.
DR Proteomes; UP000003704; 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-EC.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
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; PF00069; Pkinase; 1.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF14559; TPR_19; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 2.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000003704};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 385..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..366
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 822 AA; 91132 MW; FC06A2207BD1E42C CRC64;
MTSSSQADSR DWAEVQRLLA ELVDLQAAER EAELARRHPS PAIARRVREL LSALDESPDY
LEARSAASPE SATPAASLAE GTQIGLWRIE RLLGRGGMGE VYLAKRADGA FEQRVAIKLV
GAHAVAHIGR FHEERRILAS LEHPGIARLL DGGVAADGRP YMAMEYVDGL NIVAWCHEHA
PDLNTRLQLF GQICNAVRYA HAHLVVHRDL KPRNILVTRD GQVKLLDFGI ARLMRTSEDD
ATAGTHPLLT PDYAAPEQLD GRPVSLATDV YGLGLVLFEL LTGVTPWRHS NSNVPTLIRR
ILDGEIPPPS RIAAQRESAP VPARLLRGDL DAIVLKALRR EPASRYETAA QLWSDIERHR
QGAPVLARSA TTRYLLGRYL RRHRWLVGST AAILLVTFAG LAAVLWQSRE LARERDGARL
EADRSRAVTD YVMLMFRNAG EQPGGGPLTA KQVLDTSARR LREQFASQPV LRDDLVEMLG
ELYLRISDYQ GAESLMRSYL EDNPNLDADV AARARASLAQ AYLGLGDTAR ARKLLDEALA
HWMLDAPRYR RELFMTRITQ SQVERSEGRM EDAINTLTAA EAEGVALYGE AHEETLTIRN
SLIIALFQNG RAEEASTKLD QVEKQIQVLD RPDPIVLSLY NSRAQVAFHQ KDFVKAEEYF
RRSIDLNRSL YGPSANLALV TQNLARLMLT LDRDSEALAL FEDALPVARR YTGPTSVLTV
RTQQGLVEAL IRLGQIERAE PLIAELLTRV ENSLGNENAL YVGSRKLRSK LLAAAGRYEE
ARRDYVFVVT AIDKLGPAGA ALSTDMPPLK EKIDAGLTGR KP
//
