ID   B6EQM5_ALISL            Unreviewed;       590 AA.
AC   B6EQM5;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Putative membrane associated protein kinase {ECO:0000313|EMBL:CAQ81002.1};
GN   OrderedLocusNames=VSAL_II0248 {ECO:0000313|EMBL:CAQ81002.1};
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275 {ECO:0000313|EMBL:CAQ81002.1, ECO:0000313|Proteomes:UP000001730};
RN   [1] {ECO:0000313|EMBL:CAQ81002.1, ECO:0000313|Proteomes:UP000001730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238 {ECO:0000313|EMBL:CAQ81002.1,
RC   ECO:0000313|Proteomes:UP000001730};
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
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   ---------------------------------------------------------------------------
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; FM178380; CAQ81002.1; -; Genomic_DNA.
DR   RefSeq; WP_012551622.1; NC_011313.1.
DR   AlphaFoldDB; B6EQM5; -.
DR   KEGG; vsa:VSAL_II0248; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034273_0_0_6; -.
DR   Proteomes; UP000001730; 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; PTHR24347:SF412; CALCIUM_CALMODULIN DEPENDENT PROTEIN KINASE I; 1.
DR   PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN 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   Kinase {ECO:0000313|EMBL:CAQ81002.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:CAQ81002.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        567..588
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          14..245
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   DOMAIN          278..551
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   590 AA;  66799 MW;  642D5456B2D7FD21 CRC64;
     MKSTLQTSKD LILRVGGNST QGKRESNQDA FIVKQTSLSE LQFKGHVACI ADGVSCSDKG
     QQASHTAVTQ FVEDYFSTPD SWGVKQAATT ILATINTWLY QQQNEHDLQH NGWLTTFSSV
     IIKSNTAHVF HVGDSRVSLY RHGKLKSLTK DHQRRGAGQH RYLTRALGMD TTIDVDYQAI
     SLEQGDLLLL TTDGVHEALN SYVLNSELTA TKEKTFPLDS IAANLCDLAI KKGSQDNCSC
     LLIDVVELPD KSPQELLERF EHYPIPPVLT VGQKIDQYRV QRILYSGVRS HVYQVMDENT
     LERYVLKAPS QQFAEDSDYL CSFIREQWIG EKVNSDRIMI IHPQLSEVSF LYHVCAYLEG
     ITLRQWMFDN PKPSLEQVRT LINGVMKAVR VLQRLHIVHR DLKPENIMIM PTGNVILIDF
     GAATADGFDE VLPTIENECP LGEINYCAPE YINGEKATHQ SDIFSIGVIC YELLAKVTLS
     DNSLPYKQTT QQYLQAKRHQ SWDYHSLLFQ REELPVWIDE AIKKACHPLP SQRYQSMSEF
     MADLTVPNPQ LLRNKKAQAL IDRDPILFWK GLSIILSITV LIELGLLLSS
//