ID A0A2N0VKD0_9BACT Unreviewed; 788 AA.
AC A0A2N0VKD0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=AAA domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CWD77_03985 {ECO:0000313|EMBL:PKD44630.1};
OS Rhodohalobacter barkolensis.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae;
OC Rhodohalobacter.
OX NCBI_TaxID=2053187 {ECO:0000313|EMBL:PKD44630.1, ECO:0000313|Proteomes:UP000233398};
RN [1] {ECO:0000313|EMBL:PKD44630.1, ECO:0000313|Proteomes:UP000233398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15182 {ECO:0000313|EMBL:PKD44630.1,
RC ECO:0000313|Proteomes:UP000233398};
RA Han S.;
RT "Rhodohalobacter 15182 sp. nov., isolated from a salt lake.";
RL Submitted (NOV-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:PKD44630.1}.
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DR EMBL; PISP01000001; PKD44630.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0VKD0; -.
DR OrthoDB; 9794577at2; -.
DR Proteomes; UP000233398; 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 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:UP000233398};
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 44..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..117
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 431..505
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 589..745
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 216..280
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 307..361
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 788 AA; 89297 MW; 1C6C2579E241E2BA CRC64;
MGQFERGNGF SANKNLYNGD YPNELDPDEI DLIKLFSIIL RYKWIIAGIT LMFTIASVIY
SYSIIPVYES DGTILIKDDQ NRYPGGGAEL SNLLSATYGI GMGSTLSNEL QVFRSRSMSF
TLANRVIQED VMKNGSRFPI LWRAFPDDST VVTRDSVATR IRNNMDIVRQ DQDTDMLRIT
FKSYSPLEAA WMVDQAIEGY TDLSQQQNRG AASSALDFLE RERELIREEL NENEQRLRVY
MNETGLIQVD EQTSAAIERI SELEAQRQEL QVRKVAVTSA ISAYEQQLDE IKPGLADQFS
DNVGTTLERY QYRLAELETE KLLLLQRNPS LRDQPDQEPY LVEIEDQIQL LRREINRIAS
TLVDESADAY IGFLSNTDNG IAGRITELRT QLIELRIEES QYLAQETAID ERMAAENEFF
NNLPDNMIEL ARLKRDAEIQ EELFLTISQQ YAETALWEQT QFGQGRPLDY AFVPDKPTEP
KKRMIVIVGF LLGGIVSLGA VFTRELFNNT LDSVDHLKER GYPLLTVIPD MTNRMKEIFG
DSKTVTIQGK SISTSLLSIT DSISPVSESF RRLHNNIIYS HPDENFKRIL ITSSAKGEGK
STVSTNLAVI LADSGKKVLI IDSDLRRPNL HKLLGENRIP GLIDTLFNDD IELSQVIRET
VVPNLDLLTT GQEPPNPSAV LQSEKLKGLI DQVEEHYDHI IIDTAPYGII TDAAPLIPIV
DGVVLIARFG ETPINELNQS IENLERVHAK IIGTVLTAYN YEKSGDYYTR SNGHYDYQRA
YKDYNRSI
//
