ID G2ZB33_LISIP Unreviewed; 655 AA.
AC G2ZB33;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN OrderedLocusNames=LIV_1796 {ECO:0000313|EMBL:CBW86281.1};
OS Listeria ivanovii (strain ATCC BAA-678 / PAM 55).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=881621 {ECO:0000313|EMBL:CBW86281.1, ECO:0000313|Proteomes:UP000001286};
RN [1] {ECO:0000313|EMBL:CBW86281.1, ECO:0000313|Proteomes:UP000001286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-678 / PAM 55 {ECO:0000313|Proteomes:UP000001286};
RX PubMed=22072644; DOI=10.1128/JB.06120-11;
RA Buchrieser C., Rusniok C., Garrido P., Hain T., Scortti M., Lampidis R.,
RA Karst U., Chakraborty T., Cossart P., Kreft J., Vazquez-Boland J.A.,
RA Goebel W., Glaser P.;
RT "Complete genome sequence of the animal pathogen Listeria ivanovii, which
RT provides insights into host specificities and evolution of the genus
RT Listeria.";
RL J. Bacteriol. 193:6787-6788(2011).
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; FR687253; CBW86281.1; -; Genomic_DNA.
DR RefSeq; WP_014093164.1; NZ_CVPH01000006.1.
DR AlphaFoldDB; G2ZB33; -.
DR GeneID; 57076804; -.
DR KEGG; liv:LIV_1796; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_000288_135_2_9; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000001286; 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-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 3.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.60.40.2560; -; 1.
DR Gene3D; 3.30.10.20; -; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1.
DR Pfam; PF12330; Haspin_kinase; 1.
DR Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF21160; PrkC-like_PASTA-like; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 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}; Kinase {ECO:0000313|EMBL:CBW86281.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:CBW86281.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 339..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..271
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 363..430
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 431..499
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 500..566
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 527..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 655 AA; 72205 MW; 10BA601D67E63FE7 CRC64;
MMIGKRLNDR YKILHAIGGG GMANVYLAHD IILDRDVAVK ILRIDLADES NLIRRFQREA
QSATSLVHPN IVSVYDVGEE NDLHYIVMEH VDGMDLKQYI HENHPISYEK AVDIMLQIVS
AVAVAHQHHI IHRDLKPQNI LIDHDGVVKI TDFGIAMALS ETSITQTNSL LGSVHYLSPE
QARGGMATQK SDIYSLGIVL YELLTGKVPF DGESAVSIAI KHLQADIPSA RTQNPEIPQS
LENIIIKATA KDPFLRYQNA EEMEKDLQTC LNKDRLNEPK YVFKADDGDT KTIPIIATKE
AMQNLDNTIV PEGKVAAEEV TEEDKKGKKK KKMSKKKKIA WIVFSVIIAF TIAILLLWML
GKGPEEIAVP DVSGKTEDQA IALLQKDGFV IGKTAEKNSD EVEEGKVINT DPDAGEMKEK
GTKVNLFVSI GSKKITMDDY TGRSYDDTKA LLEEQGFKNI SSEEAYSSEV DKGMIISQTP
SAGTNVVAKS TDVKFVVSKG VEPITLKDLR GYTKTAVEDY ASPLGLKVSS SEENSDSVEK
GQVISQSPSS GTTMNPGDTI EIVISAGPKE KAVKEVTKTF NISYTPSDEE NPEPQHIQIY
IQDKDHSMTS AYREMNISQN TSVEVTFQIE EGTSGGYKII SDDKVIDEGT VPYPN
//
