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Database: UniProt
Entry: W4M3Z9_9BACT
LinkDB: W4M3Z9_9BACT
Original site: W4M3Z9_9BACT 
ID   W4M3Z9_9BACT            Unreviewed;       763 AA.
AC   W4M3Z9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=AAA domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ETSY2_29330 {ECO:0000313|EMBL:ETX04342.1};
OS   Candidatus Entotheonella gemina.
OC   Bacteria; Nitrospinae/Tectomicrobia group; Candidatus Tectomicrobia;
OC   Entotheonella.
OX   NCBI_TaxID=1429439 {ECO:0000313|EMBL:ETX04342.1, ECO:0000313|Proteomes:UP000019140};
RN   [1] {ECO:0000313|EMBL:ETX04342.1, ECO:0000313|Proteomes:UP000019140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSY2 {ECO:0000313|Proteomes:UP000019140};
RX   PubMed=24476823; DOI=10.1038/nature12959;
RA   Wilson M.C., Mori T., Ruckert C., Uria A.R., Helf M.J., Takada K.,
RA   Gernert C., Steffens U.A., Heycke N., Schmitt S., Rinke C., Helfrich E.J.,
RA   Brachmann A.O., Gurgui C., Wakimoto T., Kracht M., Crusemann M.,
RA   Hentschel U., Abe I., Matsunaga S., Kalinowski J., Takeyama H., Piel J.;
RT   "An environmental bacterial taxon with a large and distinct metabolic
RT   repertoire.";
RL   Nature 506:58-62(2014).
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:ETX04342.1}.
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DR   EMBL; AZHX01001243; ETX04342.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4M3Z9; -.
DR   PATRIC; fig|1429439.4.peg.4974; -.
DR   HOGENOM; CLU_009912_2_1_7; -.
DR   Proteomes; UP000019140; 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   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:UP000019140};
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        33..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        482..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          19..106
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          570..731
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   COILED          230..300
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          378..460
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   763 AA;  86173 MW;  6B9B2B1A790C1D3A CRC64;
     MNFFRKLYQS LAVRAQKILD IHDYVGVCWR RKWLIILPLC LGACMAALYS YTVIPMYRSS
     SLLIVEGQQI SKDYVPTASA SNLSERLGIL KQQILSRTNL ERVIRQFGLH RAQVLNETEP
     EGWVDQIKSR VKTLLANAGF NVPKPVAVPD PEGIPERVVA QFRDRIEADV VGKRRRRKSS
     YEAISVSFSG SNPHKVMGIT NAIARLFVEE NLRKGTQVVE GTTSFLNSQL TVAKQKLEQQ
     EQLLKDFKER HMGALPEQMD ANLRKLDRLQ AELQSLNEAL LKAEEKKLLY QRELREVLSR
     PAAVVEFNAP PADPRVERLK GLRQQLATLQ ARFTESYPDI PLLKNQIREL ESQLALTPPP
     AASTTEPSPP VPRVNSLQQQ LEGQLRLVQR EVAGLKAQQR DIEATRKVYE DRIEQTFSNE
     QQLNELNREI ESTRKNYREL EEKRNKAKLQ EELVKRQQGE RFDILDPAYL PLAPYKPNRK
     EMVMFGAILG GAFGFGLAFF LDFLGRDSFR KPDEIQGAFQ VPLLASVPVN DVTRRQDQLV
     TIEEPESIAS EQYRVLYTKI ERARQATSHK VIAISSAIPS DGKTISSLNL AVVMARDFGK
     KTMLLEGDFK RPSLSSYLNT KLSGGLVDVL MDGPDGPPTL VPMADTLLPF AHDNLSILPA
     VKSVRNSSHL LSSRRLQGLL DILKVQYDYI LIDTPPVLAL SDMNMYREVV DGIILVVRAE
     VTPKRAVQQT LDMLGTDKVL GFVLNGVQQS FQPYYKYYGA ISA
//
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