ID A0A225DW83_9BACT Unreviewed; 1058 AA.
AC A0A225DW83;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=FRUB_01973 {ECO:0000313|EMBL:OWK45642.1};
OS Fimbriiglobus ruber.
OC Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC Fimbriiglobus.
OX NCBI_TaxID=1908690 {ECO:0000313|EMBL:OWK45642.1, ECO:0000313|Proteomes:UP000214646};
RN [1] {ECO:0000313|Proteomes:UP000214646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP5 {ECO:0000313|Proteomes:UP000214646};
RA Ravin N.V., Rakitin A.L., Ivanova A.A., Beletsky A.V., Kulichevskaya I.S.,
RA Mardanov A.V., Dedysh S.N.;
RT "Genome analysis of Fimbriiglobus ruber SP5, the first member of the order
RT Planctomycetales with confirmed chitinolytic capability.";
RL Submitted (JUN-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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OWK45642.1}.
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DR EMBL; NIDE01000002; OWK45642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225DW83; -.
DR OrthoDB; 6111975at2; -.
DR Proteomes; UP000214646; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd14014; STKc_PknB_like; 1.
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; IPR010432; RDD.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
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; PF06271; RDD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
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:OWK45642.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000214646};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:OWK45642.1};
KW Transferase {ECO:0000313|EMBL:OWK45642.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 365..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 447..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 477..496
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 791..816
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 940..973
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 993..1011
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1017..1039
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..349
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1058 AA; 113901 MW; CC51097743A3AB6C CRC64;
MALTCPRCLR KLSDSVDPVE PPVFCMYCGQ KLRATADCPA LPPVMPDQAE TIDAPEPIYD
VSVQVEQAPP PRAADGQVAA VGSVIGGYRL GRVLGSGGMG AVYEAENETT GQRVAIKLLS
SRLSANPTSV ERFRQEGRVA SQITHPRCVF VLRADADAGR PYIVMELMPG RTLKDLVDDR
GPLPPGEAVA RILDVIDGLA EAHRCGVIHR DVKPSNCFLT DDDRVKVGDF GLSKSLDPDQ
ADQHLTQSGH FLGTILYASP EQIRGEPVGY ESDVYSVCAT LYHLLAGRAP FQHESLTAAL
ARAVSEPPPP FRAARPDVSP ELERVVLKGL DRDRARRWES LEELREELIG LQPERQAPAR
PRDMVLAFLI DLVLIQVVIL PAEVVVRFLV GTTFGLASPT EWNWPAELVY FVYFAVADGL
FGCTVGKRLA RLRVVRVGRT GPPGLRAGAV RAGVFALLTN ALMVGPEWLV EVWPRGPAGW
VLALLGAAVA VAALLLQFRR TAQGWRGVHD FASGCRVVQR PRPAHRVRLA SRFPNPLDRV
QPSPVKLPEV VGGFGVKGKI CALPDGGEVW AGVDKALGRR VLVRVFPPGR DDPVNWDAPV
TRPTRLRAVG HGTVAWNGTE RAWVGYVAPA GAPLADVIDP RGPLSWADAR LILEQLVNEL
ADAAGDGSGV YRPAVEQVWV EPGGRVQILD FPLPVGAARV PGALPEPGTG DPSDLVRRVA
TLALEGTPRA AGGRVRAPLP AHASRITDRL FGGGEPGALD ALRGALADNH AFPPHVSAGV
RAAHIGVQGP MLALGLVVMF VLGGVFNLTS ALTAVLRAQS FADTARIIES DAGCETLLER
ARRHALNAAE RERIESALRP TDRAATRRKL RQAVAVQQVE LDEIRQHLNR PERTVLTRFQ
QESADDVTDA DEISLRNVDF AVTTARAGKG ATFAAARWPM FGVFVVGVVV WPLVWAGFAL
VFRGGLAMAV AGITIVRADG RPAGRVRCAA RELLVWLPLT AVLLACLWAQ AAAPELVLAR
TVLWLAAVLM VPLYVAIALR EPARPPQDRI MGTYLVPV
//
