ID D9QR03_ACEAZ Unreviewed; 647 AA.
AC D9QR03;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Serine/threonine protein kinase with PASTA sensor(S) {ECO:0000313|EMBL:ADL12944.1};
GN OrderedLocusNames=Acear_1434 {ECO:0000313|EMBL:ADL12944.1};
OS Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Acetohalobium.
OX NCBI_TaxID=574087 {ECO:0000313|EMBL:ADL12944.1, ECO:0000313|Proteomes:UP000001661};
RN [1] {ECO:0000313|EMBL:ADL12944.1, ECO:0000313|Proteomes:UP000001661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49924 / DSM 5501 / Z-7288
RC {ECO:0000313|Proteomes:UP000001661};
RX PubMed=21304692;
RA Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Brambilla E.,
RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA Bruce D., Detter C., Tapia R., Goodwin L., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M.,
RA Spring S., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Acetohalobium arabaticum type strain (Z-
RT 7288).";
RL Stand. Genomic Sci. 3:57-65(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR EMBL; CP002105; ADL12944.1; -; Genomic_DNA.
DR RefSeq; WP_013278389.1; NC_014378.1.
DR AlphaFoldDB; D9QR03; -.
DR STRING; 574087.Acear_1434; -.
DR KEGG; aar:Acear_1434; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_000288_135_2_9; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000001661; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR CDD; cd06577; PASTA_pknB; 3.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR045269; Atg1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|EMBL:ADL12944.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001661};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ADL12944.1};
KW Transferase {ECO:0000313|EMBL:ADL12944.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 338..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..271
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 364..431
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 432..499
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 502..569
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT COILED 257..287
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 647 AA; 72828 MW; 12ACDC1B9888E98E CRC64;
MIGGCLNNRY KIEDRIGAGG MALVYEATDK LLNRRVAVKV LRPQFATDEE FIERFKREAQ
AVANFTHPNI VNIFDIGEDD GTHYIVMENV QGETLKHRIQ KQGKLDSLSA LKITKQICNA
LVTAHRKQII HCDIKPGNIL LASEDVVKLT DFGIARAVTS SSTLKQTDTV IGSAAYFSPE
QARGDKLDNR TDIYSLGIVL YEMVTGEVPF RGESPVSVAL KHIKEEPEPP TKFDNTIPAQ
IENIVLKAVS KKPQERYDNV KKMLVDVKAA LKELEELEKD NIDKSAAETD KEQEETIVMS
KNDYPTKQLS NVTDEDYREE NYIQSNKASS FCQKNRSLVI WSLVVVLIAG SLVFGYHQVI
SYFEVPVVEV PNLVEKDLET AKQSLQNKGL QLEIYNRSYN NDIPEEHIIS QYPEAGKKVK
QNRDISVAVS KGAKLIKVPG VMGKQLREAK VLIEEEDLEV GEVEYVFNDE IKKGLIVSQT
PSSNKEVKVD TEVDLIISKG KEAKPVKVPN LVGLTEENAK KRLRDFDLII GEVKYKKSLS
YFEGEVMDQE PKSGAEVVPS FPINLVVSEG IRNPYGSEVH EFNIRVNINP GEEDQRVKII
VRDDNGRRII YNQVHHPGDL VKQQIVSVGS TVVQVYVNDR LVREQRL
//
