ID I3ATX5_BIFLN Unreviewed; 766 AA.
AC I3ATX5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=HMPREF1314_1292 {ECO:0000313|EMBL:EIJ22568.1};
OS Bifidobacterium longum subsp. longum 35B.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1161904 {ECO:0000313|EMBL:EIJ22568.1, ECO:0000313|Proteomes:UP000004446};
RN [1] {ECO:0000313|EMBL:EIJ22568.1, ECO:0000313|Proteomes:UP000004446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35B {ECO:0000313|EMBL:EIJ22568.1};
RX PubMed=23682142;
RA Shkoporov A.N., Efimov B.A., Khokhlova E.V., Chaplin A.V., Kafarskaya L.I.,
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Sutton G., Weibel D.B.,
RA Nelson K.E., Smeianov V.V.;
RT "Draft Genome Sequences of Two Pairs of Human Intestinal Bifidobacterium
RT longum subsp. longum Strains, 44B and 1-6B and 35B and 2-2B, Consecutively
RT Isolated from Two Children after a 5-Year Time Period.";
RL Genome Announc. 1:E00234-E00213(2013).
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:EIJ22568.1}.
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DR EMBL; AJTI01000118; EIJ22568.1; -; Genomic_DNA.
DR AlphaFoldDB; I3ATX5; -.
DR PATRIC; fig|1161904.3.peg.1723; -.
DR Proteomes; UP000004446; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45832:SF24; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-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; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EIJ22568.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:EIJ22568.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 435..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..283
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 475..548
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 624..690
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 350..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 81120 MW; FFA8FCE27032C83B CRC64;
MIKGTVRYNM SENEPAQMIE GRYRIVRNIA EGGMATVYEA VDERLGRTVA IKVMHTQLAK
GPHREQFVER FRREANSAAS IANPHIVQVY DTGEFNGLDF LVMEYVHGVN LRHEMNTQGT
FSVRETLRVV AETLDGLASA HRAGVVHRDI KPENILINDR GHVQITDFGL AKAASQATLS
STGMLLGTAA YLAPEMIENN QATAQGDLYS VGIMAWEMMT GKVPFDSDNP VTLVFKHVHE
DVPSVATVCQ GIDPSVAAFI AHLTARQVDA RPADGAAAAE ELSQLAAKLP LEAWQYRLHA
EPIGGDHTDA TAAALVGNIA EQAPLTGVPA GAATFEPSVP AFLVDDAASN TADTGGAADV
NPPAPPVAPT TALDSSMLAD ASAPHKTQIM AQSGSETQVL PQAGDAFTRA LALSDEPDVA
SNGTGPKKQR SKKPLIIVLV IVLVLAAIGG TAGWWWFAGP GSYWSVPKPD DVTCDANAGT
ECSLAGADWA TYESTLKALG IPYKTHKEYN DDVAEGKIIS SSVNKTKAVV NSRISKRANQ
ELTVVVSKGV RMATIPKDIL DANSANGKDP LNALKRAGFD NVKHDESKDE YSMDTPQGVA
LTISPDPGTT AKHNDEVTVT LSKGPMPVTM PNIVGKTQDE MQAALGELKL TANVTEQYDD
KVEAGQVISA SQEAGAQLKW GDSVDVVISK GPEMATIPSG LVGKQESAVT KTLEALGFEV
KTDKVLGGLF GTVRTVKSGD TDLSNGGKIR LRDANGNPTV ITLAIV
//
