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Database: UniProt
Entry: A0A317CK88_9GAMM
LinkDB: A0A317CK88_9GAMM
Original site: A0A317CK88_9GAMM 
ID   A0A317CK88_9GAMM        Unreviewed;       742 AA.
AC   A0A317CK88;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Capsular biosynthesis protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DKT75_01765 {ECO:0000313|EMBL:PWQ98916.1};
OS   Leucothrix arctica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Leucothrix.
OX   NCBI_TaxID=1481894 {ECO:0000313|EMBL:PWQ98916.1, ECO:0000313|Proteomes:UP000245506};
RN   [1] {ECO:0000313|EMBL:PWQ98916.1, ECO:0000313|Proteomes:UP000245506}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC9719 {ECO:0000313|EMBL:PWQ98916.1,
RC   ECO:0000313|Proteomes:UP000245506};
RA   Choi A., Baek K.;
RT   "Leucothrix arctica sp. nov., isolated from Arctic seawater.";
RL   Submitted (MAY-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWQ98916.1}.
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DR   EMBL; QGKL01000009; PWQ98916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317CK88; -.
DR   OrthoDB; 9775724at2; -.
DR   Proteomes; UP000245506; Unassembled WGS sequence.
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:UP000245506};
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        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          42..134
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          404..477
FT                   /note="Tyrosine kinase G-rich"
FT                   /evidence="ECO:0000259|Pfam:PF13807"
FT   DOMAIN          556..688
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          224..288
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   742 AA;  81412 MW;  15A59577D1A8798C CRC64;
     MSIDSNQRLP SRVPNNQPLN GQVAPHPSTI YPEELLAPSN GLNLKDFIGI LSRRKWLVAI
     TVLLTLLAVI LITLMIKPVY RANSTIQIER NAAGLSSTNG MFQSVESRSD KDFHETQRQL
     IQSKTLARRV INQLGLDAKD TSFGVIASIK GALGASQENQ SSKERTEALF LDNLTVQPVS
     NSQLVQINYD STDPKLAADI ANAISKTFVR MNLEKRFNVA TFSKEFLTEQ TQEVRATLER
     SEQALNAYAR EYGIVQDSEG ENTDTQSLKS LSQELVSAQR DRIQAQALLA QAEGTDSQDP
     STIAILSKDP KMQDKGTQLL QLVAERNALI KKSSSGTSRA IRRLESQVTR LRAEINAHAS
     TVIATLRVEA ESANKRQELI KTQLTALKNT AITTAGDSIR YNTLKREVES NRTIYKELLQ
     QYKNAKVNGE NGTNNITIID KAGVPYEKYK PRLRNNLAFG LLLGLMLGMG AAFLREFMDD
     TLKSSDELER ITGLPVLGLL PNIKNQSDDQ VALLAHMEPR SPLAEAIRSL RTSLKFSTQY
     GAPRVTFITS SNPSEGKSSI ALNLATAYAQ VGGKVLLIDA DLRNPSLHHL LKLDNLEGLT
     NYLAGAGEAE NISRPCLIKQ LRVITSGPIP PDPVELLSGK RMQALLDAST EEFDHIIIDG
     PPVIGLADAL VLSNLADATI LSVQAGKTRK ASLLATLKRL ERTSGNIIGT LLSRVDQSSN
     PEYSEDSYYT YTNSTKYNNS NS
//
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