ID A0A1F1I840_9MICC Unreviewed; 783 AA.
AC A0A1F1I840;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=HMPREF2863_01655 {ECO:0000313|EMBL:OFR87863.1};
OS Micrococcus sp. HMSC067E09.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Micrococcus.
OX NCBI_TaxID=1739367 {ECO:0000313|EMBL:OFR87863.1, ECO:0000313|Proteomes:UP000177882};
RN [1] {ECO:0000313|EMBL:OFR87863.1, ECO:0000313|Proteomes:UP000177882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC067E09 {ECO:0000313|EMBL:OFR87863.1,
RC ECO:0000313|Proteomes:UP000177882};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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:OFR87863.1}.
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DR EMBL; LTYF01000054; OFR87863.1; -; Genomic_DNA.
DR RefSeq; WP_070637517.1; NZ_KV809416.1.
DR AlphaFoldDB; A0A1F1I840; -.
DR STRING; 1739367.HMPREF2863_01655; -.
DR Proteomes; UP000177882; 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-EC.
DR CDD; cd06577; PASTA_pknB; 2.
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; 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; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 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; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000177882};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 408..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..278
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 433..499
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 567..635
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 288..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..747
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..783
FT /note="Pro residues"
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 783 AA; 80397 MW; 3045C0D634A52F21 CRC64;
MSTEHILNGR YRMEDLIGRG GMADVYRGTD LRLKRTVAIK MMRPDLARDP QFQSRFRREA
TSSASLNHPN IVHVFDTGEE DIEDRHAHEV SCPFLVMEHV DGGTMKDAIG AGDVTVEEAV
AWLDGVLAAL SYSHGLGIVH RDIKPANVMV TGSGEVKVMD FGIARALADT SATMTQTQTV
VGTAQYLSPE QAMGGTVGTR SDLYSVGCVA FELLTGRPPF LGESPVSVAY QHVRQDPPRP
STLNPDVTPA LDAVVLTALA KEPDDRFDDA DQFAAALVEA LGSPEQTQTG ALPLVDPDAD
APAGPTPSED STPALPAAGA ATGAGAAGAA AGSGAAGAAA GAAAVGSTAA GAAGASVDSG
GHRPPLTPRS LSTVDTNRHL PVRADLPNTG STAVGDAEEE RSPRRRGLLF GLIALLLLAV
AAAVALPLLL GGRDSQVEVP DVVGVPVEQA ETTLTEAGLE TRTSEVYDDE VPEGSVVSTD
PGAGDRVDSG SEVRLKVSQG PSSVTLPESL RGASEATVRD ELSRLGLTVS SVSSTNSADV
PRDRLVSTSP ELGSAVPPGS SVDLQLSTGR TTLPNVVGLS EESARTALQE AAPNVIVRVQ
ERESAAATPG YVMRQDPPAD REVDNEGAVT LTVAKAAPEP SETPSPSDDP EPSPSQSPTP
SEDPTESPDP SPSPSQSPDP TDSPEPSESP SPSDDPEPSE SPSPSEDPTE SPEPSDSPPP
SEDPTESPDP SPSPSQSPDP TNSPTPSESP SPTGSGSPSS PEGRPTRPGP PSDVPSNGPA
PRD
//
