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Database: UniProt
Entry: A0A402CRM4_9BACT
LinkDB: A0A402CRM4_9BACT
Original site: A0A402CRM4_9BACT 
ID   A0A402CRM4_9BACT        Unreviewed;       504 AA.
AC   A0A402CRM4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
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=CCAX7_002000 {ECO:0000313|EMBL:BDI28149.1}, CCAX7_11850
GN   {ECO:0000313|EMBL:GCE52671.1};
OS   Capsulimonas corticalis.
OC   Bacteria; Armatimonadota; Armatimonadia; Capsulimonadales;
OC   Capsulimonadaceae; Capsulimonas.
OX   NCBI_TaxID=2219043 {ECO:0000313|EMBL:GCE52671.1};
RN   [1] {ECO:0000313|EMBL:GCE52671.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX-7 {ECO:0000313|EMBL:GCE52671.1};
RA   Li J., Tonouchi A.;
RT   "Draft Genome Sequence of Capsulimonas corticalis strain AX-7.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2018).
RN   [2] {ECO:0000313|EMBL:BDI28149.1, ECO:0000313|Proteomes:UP000287394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX-7 {ECO:0000313|EMBL:BDI28149.1,
RC   ECO:0000313|Proteomes:UP000287394};
RA   Li J., Kudo C., Tonouchi A.;
RT   "Capsulimonas corticalis gen. nov., sp. nov., an aerobic capsulated
RT   bacterium, of a novel bacterial order, Capsulimonadales ord. nov., of the
RT   class Armatimonadia of the phylum Armatimonadetes.";
RL   Int. J. Syst. Evol. Microbiol. 69:220-226(2019).
RN   [3] {ECO:0000313|EMBL:BDI28149.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AX-7 {ECO:0000313|EMBL:BDI28149.1};
RA   Li J., Tonouchi A.;
RL   Submitted (MAY-2022) 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   -!- SIMILARITY: Belongs to the anti-sigma-factor family.
CC       {ECO:0000256|ARBA:ARBA00037972}.
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DR   EMBL; AP025739; BDI28149.1; -; Genomic_DNA.
DR   EMBL; BHFQ01000002; GCE52671.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A402CRM4; -.
DR   KEGG; ccot:CCAX7_002000; -.
DR   InParanoid; A0A402CRM4; -.
DR   OrthoDB; 453368at2; -.
DR   Proteomes; UP000287394; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   PANTHER; PTHR35526; ANTI-SIGMA-F FACTOR RSBW-RELATED; 1.
DR   PANTHER; PTHR35526:SF1; SERINE-PROTEIN KINASE RSBW; 1.
DR   Pfam; PF13581; HATPase_c_2; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022527}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287394};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        48..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        78..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        119..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        274..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          367..479
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF13581"
SQ   SEQUENCE   504 AA;  54237 MW;  E060A6E135B2D792 CRC64;
     MVIPISRSQN QLPALILFCG VLATLLGVTV LIGWHTHNLT LLKIYPSFVA MAYNTALGFL
     LSGIALIAGV FEKRRITLAC GVLLTLIGGL TIAEYLFGVN LGVDELLMRS YVRSGILHFG
     RMAIATASCF TAFGVAQTVW ALRRGAYPPI FLALIGATVT ALGAVAFTGY FIGVTEAYRW
     GQFTRMAVHT SLGFIVLGAG ALCEAWLAEV RRGVSRPHWL PFVATIFGSA ASVSLWQALV
     VDQSGNLAII HQYSQAHPGL GQYVQAQSRL PYEALAGGVL VSCLLGWSVY LAQRASERAE
     MLSKAGEELE HRVQERTEDL DRTNQALQEV LTCVSNGRLK LCLTEAALPP SRSIVSSSVE
     LSRTSGLKAL RDLARQAALE ASLPVERIDD LVTAVSEASM NAVVHGGGGH GEVRLSTDDR
     IQVWVRDFGS GITLDHLPRA TLERGYTTAG TLGHGFWLML STVDHLFLLT GPAGTTLVLE
     QGKEEPLPPW LLQQINDNPP ALAA
//
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