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Database: UniProt
Entry: A0A1Q2M7S2_9GAMM
LinkDB: A0A1Q2M7S2_9GAMM
Original site: A0A1Q2M7S2_9GAMM 
ID   A0A1Q2M7S2_9GAMM        Unreviewed;      1032 AA.
AC   A0A1Q2M7S2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=AAA domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Mag101_14670 {ECO:0000313|EMBL:AQQ68736.1};
OS   Microbulbifer agarilyticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Microbulbiferaceae; Microbulbifer.
OX   NCBI_TaxID=260552 {ECO:0000313|EMBL:AQQ68736.1, ECO:0000313|Proteomes:UP000188219};
RN   [1] {ECO:0000313|EMBL:AQQ68736.1, ECO:0000313|Proteomes:UP000188219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GP101 {ECO:0000313|EMBL:AQQ68736.1,
RC   ECO:0000313|Proteomes:UP000188219};
RA   Jung J., Bae S.S., Baek K.;
RT   "Genome of Microbulbifer agarilyticus GP101.";
RL   Submitted (FEB-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; CP019650; AQQ68736.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2M7S2; -.
DR   STRING; 260552.Mag101_14670; -.
DR   KEGG; maga:Mag101_14670; -.
DR   OrthoDB; 9775724at2; -.
DR   Proteomes; UP000188219; Chromosome.
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:UP000188219};
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        32..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        440..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          17..107
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          388..459
FT                   /note="Tyrosine kinase G-rich"
FT                   /evidence="ECO:0000259|Pfam:PF13807"
FT   DOMAIN          531..681
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   REGION          969..1032
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          348..382
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1006..1032
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1032 AA;  114734 MW;  055DFEB69453534D CRC64;
     MNYAQGNGGD ELPQEQSLDL LRYWKILFAK RWLIFGLSVA MSAVAIAFIY KMPSRYQATA
     SLVFEVDQAN PVSVEEIYDL GAQRRDYILT QTEMLKSRQL AERVIQRLNL VNHPEFAAQS
     KSGLFGLFSK DSASDSSMSA KAETATLDNV TSAFLKRLTI SPARNTNLVK VQFEAKSAKL
     SADVANALVE EFIFFQSEAK EQFTNRATSW LNERQETLRS KLEASEQNLQ NFRETEDLVD
     LSGVRGLSEQ DLNAATTQLQ ETRREFKQIA SVFNQFERLK GNELALANLP EVISNPLIQE
     IKRNEAAAER NVSELARRYK PKHPTMIAAS NELDMIRDQL ASEVRILADS IESQYNTAQA
     RVAAQEQEVQ RAKAAYQNVS QKEFRYQELV REVEANRQLY DTFFTRANET REASGFEIAP
     ARFLDSAVIP NTATKPNKKL LAMMAIALSA VFATAIALLL DFLRMGVRSP EDVEVHLGQN
     LIGLLPQVST PKDSKLNLRT FFDPNHYTFS EAVRTLRTGV VLTGLGKSMR TILITSSVPA
     EGKTTVAENL AFALSQVERV LLVDLDLRKP TVAADFRIAS NHPGITDLIQ GNKPLEECVY
     KDIGSNLHVM PSGGHLTDPQ QLLVSPRFSE TISSLAQDYD RIVIDSPPVQ AVSDALIISH
     LADALLYVIK YDSTNKRTVS RGIERLTKIN SKIDGIVLTH VDTSKDAIYA DEYYDYDYGN
     SRRDRKPVAP TVASSQALGA VSSPRVHTDT VSTRIAAEPK SDTYAVSRSN IHTDHTPVHT
     ANSETTVANE LVEDDVAVVA EPEYQMVAEP EVTTEVENAF VAMEAAVDVE EQHATEAEID
     PAETVFVRAE DHVPDDLISD ADVVAGSDVS TDSEFTQESI QSAVEEAAHE AIHETIHEDI
     QEAVQESIRE DSQEAYQGRL TQSSLDRIVE AEKATSYFSA PTSLEDDTAD ASIDRELLSD
     VTPHEISQEI PQFEVEKLAE EDTSSEVDLE DGSTSVTDEK SKKKSRSPRS QRSRAKKKQR
     KKRARAKRRA AK
//
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