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Database: UniProt
Entry: S0EU24_CHTCT
LinkDB: S0EU24_CHTCT
Original site: S0EU24_CHTCT 
ID   S0EU24_CHTCT            Unreviewed;       743 AA.
AC   S0EU24;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Capsular exopolysaccharide family {ECO:0000313|EMBL:CCW35088.1};
GN   ORFNames=CCALI_01270 {ECO:0000313|EMBL:CCW35088.1};
OS   Chthonomonas calidirosea (strain DSM 23976 / ICMP 18418 / T49).
OC   Bacteria; Armatimonadota; Chthonomonadetes; Chthonomonadales;
OC   Chthonomonadaceae; Chthonomonas.
OX   NCBI_TaxID=1303518 {ECO:0000313|EMBL:CCW35088.1, ECO:0000313|Proteomes:UP000014227};
RN   [1] {ECO:0000313|Proteomes:UP000014227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23976 / ICMP 18418 / T49
RC   {ECO:0000313|Proteomes:UP000014227};
RA   Lee K.C.Y., Morgan X.C., Dunfield P.F., Tamas I., Houghton K.M.,
RA   Vyssotski M., Ryan J.L.J., Lagutin K., McDonald I.R., Stott M.B.;
RT   "Genome sequence of Chthonomonas calidirosea, the first sequenced genome
RT   from the Armatimonadetes phylum (formally candidate division OP10).";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00001074};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the etk/wzc family.
CC       {ECO:0000256|ARBA:ARBA00008883}.
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DR   EMBL; HF951689; CCW35088.1; -; Genomic_DNA.
DR   RefSeq; WP_016482629.1; NC_021487.1.
DR   AlphaFoldDB; S0EU24; -.
DR   STRING; 454171.CP488_02825; -.
DR   KEGG; ccz:CCALI_01270; -.
DR   PATRIC; fig|1303518.3.peg.1294; -.
DR   eggNOG; COG0489; Bacteria.
DR   eggNOG; COG3206; Bacteria.
DR   HOGENOM; CLU_009912_2_1_0; -.
DR   InParanoid; S0EU24; -.
DR   OrthoDB; 9794577at2; -.
DR   Proteomes; UP000014227; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05387; BY-kinase; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR025669; AAA_dom.
DR   InterPro; IPR032807; GNVR.
DR   InterPro; IPR003856; LPS_length_determ_N_term.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005702; Wzc-like_C.
DR   NCBIfam; TIGR01007; eps_fam; 1.
DR   PANTHER; PTHR32309; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR32309:SF13; TYROSINE-PROTEIN KINASE ETK-RELATED; 1.
DR   Pfam; PF13614; AAA_31; 1.
DR   Pfam; PF13807; GNVR; 1.
DR   Pfam; PF02706; Wzz; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014227};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   TRANSMEM        27..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..97
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          373..444
FT                   /note="Tyrosine kinase G-rich"
FT                   /evidence="ECO:0000259|Pfam:PF13807"
FT   DOMAIN          518..636
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   REGION          708..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          211..245
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          364..398
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   743 AA;  81440 MW;  4AEAEB5EC0E3D69F CRC64;
     MNAPQMIVDA TPTPDARDAL GVVWRRGWAF IVVLALCLGV TALVNKYMPK KWTAQATLLV
     QPQPPSLVGA DQSTRNAVET ETPATEMQLL QSEQIAARSL DWAQRHANGL TVPSMSTKEF
     LDRLDIENPQ NTQLINISFE YGNPQIATLM ANAVANAFLQ YKRELVEEYA TGAINSLSQR
     VAMAKAKYDA ALAAETQFKE QHNLTDIGAQ QTALLSNYHN LQDQISQLQA KIAGEQQTYN
     LYKKQLAAEN SAILTAKTVI DPETVSQDIQ QYNAAQQQLE QDKLKYTPLY PGVIPNDEAR
     VKMLKQKLDQ DLAAITNSKV PSLNNHTQLQ QNYYQAMTAL LADQKQLGQM MEQSAGIAAK
     LRDLPALYEQ YQKLEQRYQS AENVYQQLRN DLDAADANRA AAQPNIQIAQ LATVPTDPSS
     PRIRFNFGIG ALIGVILGIT VMLLLEQNDS RMRSLKLARQ MLPGPVIGTL PRISGSHIRA
     LEAGEPAGPI AEAYSLARAN LALALRDLRH EDLEGSQVVM VTSALPGEGK SITVASLARS
     AARAGKRVIL INADLRRPAM NQIFRTNEKI GLAEVLIGAV SVEDALVSSD TPYLTILHSG
     TPDRNPSDLL ALPTMSELIA YLRKEADLIL IDTPPCSVVA DALVLAPLCD CILQVVSLDM
     ADQVTTLETA EALRAAEPKK LLFFINRSDT RANRNYHSYY YYNKNGASAR NGHTPDKDKP
     SVPSLAPETN VSGEMALPQE EEG
//
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