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Database: UniProt
Entry: A0A3E0VF83_9MICO
LinkDB: A0A3E0VF83_9MICO
Original site: A0A3E0VF83_9MICO 
ID   A0A3E0VF83_9MICO        Unreviewed;       499 AA.
AC   A0A3E0VF83;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=AAA domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B7R54_03085 {ECO:0000313|EMBL:RFA08319.1};
OS   Subtercola boreus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Subtercola.
OX   NCBI_TaxID=120213 {ECO:0000313|EMBL:RFA08319.1, ECO:0000313|Proteomes:UP000256486};
RN   [1] {ECO:0000313|EMBL:RFA08319.1, ECO:0000313|Proteomes:UP000256486}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K300 {ECO:0000313|EMBL:RFA08319.1,
RC   ECO:0000313|Proteomes:UP000256486};
RA   Cho Y.-J., Cho A., Kim O.-S., Lee J.-I.;
RT   "Comparative genome analysis of Subtercola boreus.";
RL   Submitted (APR-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:RFA08319.1}.
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DR   EMBL; NBWZ01000001; RFA08319.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E0VF83; -.
DR   OrthoDB; 9812433at2; -.
DR   Proteomes; UP000256486; 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:UP000256486};
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        175..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          3..88
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          273..417
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   REGION          463..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..484
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   499 AA;  53210 MW;  3791336DABAE7AA0 CRC64;
     MQLQDILRVL QRSWILIVGL TVLGLLAAGA ALAVTAPQYQ STSRLFVSTQ ATDNASNALQ
     GSTYTQNRMI SYSHLVVQPI VLDPVIAALG LDLTADQLAS HVSADVITDS LILEVTVTEP
     SAQQSADIAN AIATQLVTTI TTQIEDPGDG TKPLIAVSII ADASVATSPT SPLPWLYLLV
     GGVGGLLLSV GLAFLIAGFD NRVRSIDDLK RLTDLPVLGH FPRQNTAREK PLLLADDMMS
     QRAESFRALR TNLQYFDLAT TNQVLLFTSS IPGEGKTTTS LNLAITLAQT GKRVIYIECD
     LRRPKSAKYL NIEGAVGLSD VLVSRVALDD VLQAGVVETL TILPAGSLPP NPSELLGSEQ
     FASLLSSMRL LYDYVILDAP PLLAVTDAAI LSRESDGVIV VVGTSLVNRQ QVETSIDILT
     QVDAHVLGVA ANFLPRRGVD AYSYYTYGYV ALSAVRDARV PGAADRSDDP SAAPADDRIS
     DVAHATRRAA TSAERLTRR
//
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