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
//