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Database: UniProt
Entry: A0A238Z126_9ACTN
LinkDB: A0A238Z126_9ACTN
Original site: A0A238Z126_9ACTN 
ID   A0A238Z126_9ACTN        Unreviewed;       483 AA.
AC   A0A238Z126;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Capsular exopolysaccharide family {ECO:0000313|EMBL:SNR77067.1};
GN   ORFNames=SAMN06272737_12424 {ECO:0000313|EMBL:SNR77067.1};
OS   Blastococcus mobilis.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1938746 {ECO:0000313|EMBL:SNR77067.1, ECO:0000313|Proteomes:UP000198403};
RN   [1] {ECO:0000313|EMBL:SNR77067.1, ECO:0000313|Proteomes:UP000198403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44272 {ECO:0000313|EMBL:SNR77067.1,
RC   ECO:0000313|Proteomes:UP000198403};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZNO01000024; SNR77067.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238Z126; -.
DR   OrthoDB; 9812433at2; -.
DR   Proteomes; UP000198403; 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; 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; 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   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:UP000198403};
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        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..89
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          272..401
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   REGION          143..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   483 AA;  50717 MW;  2BA499E3F44D34C2 CRC64;
     MQGNVTLRSL RDHSYFIVLG VLLGLGAAGL LTWTTERTYT SSTQLFVGAV GATDTADAYE
     GNLFSQERVA SYAQILTSPD LAERVVDELG LDLTAGELAA KVTAAPVPET VVLEVKVTDT
     SAERAQAIAT SLGRQFASRV TELETPAGAS SSTVAVSTIQ TPDFNPEPAS PDVPGTLGRG
     AAIGLVLGTG VALLRTRTDR AVRRDDDVEE AAGAHVVGRV LEQHRWARTR LPADVFGQSP
     AAEAYRALRV NLRHLDGRRR PQAVVVTGPL PGAGASTVAV NLSASLAASG QRVLLIDGDL
     RRPRVTHCLG LPDGPGLTDV LTGSAELHDV VRPWRGGRLS VLGAGPLPSD PEALLGSARM
     RSLLDVLRDQ YDQVILDAPP LLSVVDAAVL SAVADSCLLV ARYGRTRREH LAEAAAMVTR
     VRVPSLGVVL NRVPRRAAVG SPGARGYRAE GHRRTTETMV AGSSADPDAR PGAGAPDRLP
     PHE
//
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