ID   B7VTW7_VIBA3            Unreviewed;       611 AA.
AC   B7VTW7;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Serine-threonine protein kinase {ECO:0000313|EMBL:CAV26896.1};
GN   OrderedLocusNames=VS_II1030 {ECO:0000313|EMBL:CAV26896.1};
OS   Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=575788 {ECO:0000313|EMBL:CAV26896.1, ECO:0000313|Proteomes:UP000009100};
RN   [1] {ECO:0000313|EMBL:CAV26896.1, ECO:0000313|Proteomes:UP000009100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LGP32 {ECO:0000313|EMBL:CAV26896.1,
RC   ECO:0000313|Proteomes:UP000009100};
RA   Mazel D., Le Roux F.;
RT   "Vibrio splendidus str. LGP32 complete genome.";
RL   Submitted (FEB-2009) 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};
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DR   EMBL; FM954973; CAV26896.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7VTW7; -.
DR   STRING; 575788.VS_II1030; -.
DR   KEGG; vsp:VS_II1030; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034273_0_0_6; -.
DR   Proteomes; UP000009100; Chromosome 2.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00143; PP2Cc; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF13672; PP2C_2; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51746; PPM_2; 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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAV26896.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        588..608
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          37..271
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   DOMAIN          304..566
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   611 AA;  69150 MW;  C85B2A31808F6B46 CRC64;
     MSRKREEEQL RRRPVMTISF SQGQVITPES NNQLTLKFGG YSNQGVRDEN QDAIIVKHPI
     TRAEQELKGS VACVADGASC SEHGQKASHT SVMQFIDDYY ATPQSWSIQR SAQKVLTSLN
     SWLFNTSVSN IHPAQQVNHN ALVSTFSSVI LKSNTAHIFH VGDSRIYLLR DGELRQLTRD
     HTRKNMGQKH YLTRALGMDN QLNVDYQTLP IKKNDCFILT SDGVHEFVSP NTFNEHIDKP
     GADFEYAAQT ICNTALSHNS SDNVSCLLVQ ISHLPKPSLI EFHEKLAKRA IPPALKLGQS
     IDNFMVLEVL YAGSRSHVYR VMQKETQTEF VLKVPSVQYH DDPAQLRAFF NEQWAGILLK
     NKRVMKVYPT PENSQFLYQI CEWVEGITLR QWMYDNPKPS LNEVRDILEK ITQGIRVLQR
     ADMVHRDLKP ENIMLQHDGE IKIIDLGAVL VRGLEEGELA DKDDTPLGAV NYIAPETIKH
     NTATTSSDLF SIAVIGYEML TGELPYSEMT AQSLKQSRHH QWEYQPITQK RADLPSWVDL
     VLQKACAESP SERHQVLGDF VADLYTPNQS LVESKAKQPL INRNPIQFWK VLALLLGIVA
     IVELGLLLNS S
//