ID A0A370MZA9_9BURK Unreviewed; 540 AA.
AC A0A370MZA9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Peptidase C55 {ECO:0008006|Google:ProtNLM};
GN ORFNames=DLM46_32510 {ECO:0000313|EMBL:RDJ98718.1};
OS Paraburkholderia lacunae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2211104 {ECO:0000313|EMBL:RDJ98718.1, ECO:0000313|Proteomes:UP000254875};
RN [1] {ECO:0000313|Proteomes:UP000254875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S27 {ECO:0000313|Proteomes:UP000254875};
RA Feng T.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-seryl-[protein] = CoA + O-acetyl-L-seryl-
CC [protein]; Xref=Rhea:RHEA:59392, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:15352, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:141128; Evidence={ECO:0000256|ARBA:ARBA00023671};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59393;
CC Evidence={ECO:0000256|ARBA:ARBA00023671};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-threonyl-[protein] = CoA + O-acetyl-L-threonyl-
CC [protein]; Xref=Rhea:RHEA:65340, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:16780, ChEBI:CHEBI:30013, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:141025; Evidence={ECO:0000256|ARBA:ARBA00023676};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65341;
CC Evidence={ECO:0000256|ARBA:ARBA00023676};
CC -!- SIMILARITY: Belongs to the acetyltransferase YopJ family.
CC {ECO:0000256|ARBA:ARBA00023785}.
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:RDJ98718.1}.
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DR EMBL; QHKS01000031; RDJ98718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370MZA9; -.
DR OrthoDB; 8945160at2; -.
DR Proteomes; UP000254875; Unassembled WGS sequence.
DR InterPro; IPR005083; Ser/Thr_AcTrfase.
DR Pfam; PF03421; Acetyltransf_14; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Reference proteome {ECO:0000313|Proteomes:UP000254875};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 37..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 58404 MW; F2CB41DEB066E5FF CRC64;
MRGPMIFSTS TAVHFASRAT TALQNLPAMS DIRCNGAATK HSGGSMPNRI PSNAISHLPS
PTAAAQTEPR QAQPGQKQLR KAGSVFSGLK RRISACVRPV VTPPNDGNAS APSQAPAPRP
RLAAVPGVGV TRLQESVGLD ARIELRFRRG SDAGGAASAG IEALHVPLRD VGFGAGLIAH
APQQNADSST ASARHFAIAR LDQVKAHFQA LLLGNWSPGP TDDKYDAAIL PAIVAAENDR
SPALNLTLLS PKEDFASWLK ATRPARARVM FPMPGNDAHY VTADIRRIGG KTSVIVIEPL
SLKDNADLKD STRDKYEKRT LPLLKKALKS DVTLSVLTVD TQKSTNDCRV FALSAAAKLA
DNAFLIDSLH QQNLSRQPIR TALGQDAEVL ASTRKVRVLD GKGILPPAFV KHSQSRTTLS
NWLKANPPAF ANAGVNKKDQ SLADRFDDHR KTRYDKPVHS RFMQDNLPDL EVQVRNLTFS
TSIEQKRLTY LDRAIEYLRH APEGECSRLL ASMGDVSNDP PGPANLRLDD RDWGPHPDSL
//
