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
//