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Database: UniProt
Entry: A0A255T7H9_9BACT
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ID   A0A255T7H9_9BACT        Unreviewed;       847 AA.
AC   A0A255T7H9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Capsid assembly protein {ECO:0000313|EMBL:OYP61168.1};
GN   ORFNames=CIL02_06900 {ECO:0000313|EMBL:OYP61168.1};
OS   Prevotella sp. P3-122.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=2024223 {ECO:0000313|EMBL:OYP61168.1, ECO:0000313|Proteomes:UP000215645};
RN   [1] {ECO:0000313|EMBL:OYP61168.1, ECO:0000313|Proteomes:UP000215645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P3-122 {ECO:0000313|EMBL:OYP61168.1,
RC   ECO:0000313|Proteomes:UP000215645};
RA   Accetto T., Nograsek B., Avgustin G.;
RT   "Comparative genomics of non-oral Prevotella species.";
RL   Submitted (AUG-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}.
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:OYP61168.1}.
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DR   EMBL; NPJH01000037; OYP61168.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255T7H9; -.
DR   OrthoDB; 9794577at2; -.
DR   Proteomes; UP000215645; 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   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:UP000215645};
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        39..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        514..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..117
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          457..530
FT                   /note="Tyrosine kinase G-rich"
FT                   /evidence="ECO:0000259|Pfam:PF13807"
FT   DOMAIN          602..729
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
SQ   SEQUENCE   847 AA;  94360 MW;  B66FB8FABEF8383B CRC64;
     MEEKKNLEME NANVPFEKEE QSAFDFAAIY TTIILNWKWF ALSLIICLGV AAIYLRYTTP
     IYQAYAKLLI KDNEGNSSRN NMLNTSTLGM ITNSNGIDNE MEILSSHSIA EQAVRDLKLY
     VNYYIKGKIK YNLLYKTQPI SVDVDPAHLE KLNAGINLDI VKEGNKYHIT GTYYVPISDN
     EADGPFAIDK TFSQLPATIG TRAGILSFSA NPGYQMQEGQ QIKVVINSPK SEAYKYVGSL
     SVSQTSKTTT IAQLVISDES PQRAVDYLKQ LAICYNRQAN EDKNEIAVRT EEFINGRLEK
     INAELGNTEG QLENYKKSHN MVELKMNAGQ AVGNADQYSQ KLAEISTQVE LLNSINDYMN
     QPDNRYQTLP SNVGLTDASA TSLINKYNEI VLQRNRLLRS ASENSPTVTP LTSQLEDLSN
     SIRRAMSQAR RNVEIQRNAI SSQFNKYQGQ IQSTPEQERM LTQIGRQQEV KSGLYLMLLQ
     KREENSISLA ATADKGKLID DPAAGGKVSP KSSLIMLIGL IAGLAIPAII LYIVQLFRYK
     IEGHDDVASL TTLPIIADVA VASETAKTKA DIVVHENKNT QMEEIFRSMR TNIQFMLKEN
     QKTIMFTSTT TGEGKTFTAA NLAVSFALLG KKVVLVGLDI RKPRLAQLFE IDDKKHGITN
     LIVKNSPNKD DILGQIVPSG INNNLDLLMA GPIPPNPAEL VARTSLDDIM GNLREMYDYI
     LIDTAPVGLV TDTLQISRVA DVTVYMCRAD YTPKESFELI NSLAAEKKLP TMCVVLNGID
     MSKKKYGYYY GYGRYGKYGR YGRYNSKSQR YGAYGSYGRY GSYGAYGSYG SYVNSHYGDK
     NDTSIKV
//
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