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Database: UniProt
Entry: A0A2S9QSB4_9MICO
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Original site: A0A2S9QSB4_9MICO 
ID   A0A2S9QSB4_9MICO        Unreviewed;       565 AA.
AC   A0A2S9QSB4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=B4915_01335 {ECO:0000313|EMBL:PRI12483.1};
OS   Leucobacter massiliensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=1686285 {ECO:0000313|EMBL:PRI12483.1, ECO:0000313|Proteomes:UP000238650};
RN   [1] {ECO:0000313|EMBL:PRI12483.1, ECO:0000313|Proteomes:UP000238650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=122RC15 {ECO:0000313|EMBL:PRI12483.1,
RC   ECO:0000313|Proteomes:UP000238650};
RX   PubMed=29204283;
RA   Leangapichart T., Gautret P., Nguyen T.T., Armstrong N., Rolain J.M.;
RT   "Genome sequence of 'Leucobacter massiliensis' sp. nov. isolated from human
RT   pharynx after travel to the 2014 Hajj.";
RL   New Microbes New Infect 21:42-48(2017).
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};
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:PRI12483.1}.
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DR   EMBL; MWZD01000012; PRI12483.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S9QSB4; -.
DR   Proteomes; UP000238650; Unassembled WGS sequence.
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   CDD; cd06577; PASTA_pknB; 2.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 2.
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:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR   Pfam; PF03793; PASTA; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 2.
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:PRI12483.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000238650};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:PRI12483.1};
KW   Transferase {ECO:0000313|EMBL:PRI12483.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        336..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..294
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          367..433
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          434..501
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   BINDING         47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   565 AA;  60267 MW;  008B433C02D7E2D2 CRC64;
     MPETSDANGE QRILAGRYAI GEFVGQGGMA TVYRGTDTKL GRQVAIKVMK ADLAGDEQFR
     SRFRQEAQSA SRMAHPTVVR VFDAGDDLIQ TADGPKRLPF IVMEYVEGTN LRQLLAEGGL
     SQSEACRVVD SVLTALEYSH RAGIVHRDIK PANIMITKSG QVKVMDFGIA RAVSETSSTL
     QQTTAILGTA AYFSPEQAKG ESIDARTDLY STAVLLYELL AGDVPFRGDT AVAVAYQHVS
     ERPTPPSDRN PEVPPELDRV VLYGLAKDRS KRFQSASEFR DALRVAASGQ MPRLALQQQD
     TVLFTGGEEI SESDLALRQL SESGGAARTQ SRPPVMWTWA AILTVGAVIV AVVFWLVTLA
     PQQFVPDNSR EVSAELVGMD RAEAMELLQK QGLLPLTIDE TSDEVPAGHV VSTDPEPGTV
     LTVGDTITLH ISTGPETAKV PEPDSLSIED YKKELSDLGL TVGVETSVDD PVAPAGRVLD
     VTPAPGTDLA SGESVSVRVA SGKVKVPDVV GHPLEGARAL LSGNGLSVTY TADPCPAADG
     FPVTWQSIVG EQPQGAVLEI KYCGS
//
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