ID A0A1I2JML7_9ACTN Unreviewed; 782 AA.
AC A0A1I2JML7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Lysine N-acyltransferase MbtK {ECO:0000256|ARBA:ARBA00020586};
DE AltName: Full=Mycobactin synthase protein K {ECO:0000256|ARBA:ARBA00031122};
GN ORFNames=SAMN05421541_11318 {ECO:0000313|EMBL:SFF55368.1};
OS Actinoplanes philippinensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=35752 {ECO:0000313|EMBL:SFF55368.1, ECO:0000313|Proteomes:UP000199645};
RN [1] {ECO:0000313|EMBL:SFF55368.1, ECO:0000313|Proteomes:UP000199645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43019 {ECO:0000313|EMBL:SFF55368.1,
RC ECO:0000313|Proteomes:UP000199645};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acyltransferase required for the direct transfer of
CC medium- to long-chain fatty acyl moieties from a carrier protein (MbtL)
CC on to the epsilon-amino group of lysine residue in the mycobactin core.
CC {ECO:0000256|ARBA:ARBA00003818}.
CC -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005102}.
CC -!- SIMILARITY: Belongs to the peptidase S45 family.
CC {ECO:0000256|ARBA:ARBA00006586}.
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DR EMBL; FONV01000013; SFF55368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2JML7; -.
DR STRING; 35752.SAMN05421541_11318; -.
DR OrthoDB; 9759796at2; -.
DR UniPathway; UPA00011; -.
DR Proteomes; UP000199645; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
DR Gene3D; 2.30.120.10; -; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 2.
DR Gene3D; 1.10.439.10; Penicillin Amidohydrolase, domain 1; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR019432; Acyltransferase_MbtK/IucB-like.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023343; Penicillin_amidase_dom1.
DR InterPro; IPR043146; Penicillin_amidase_N_B-knob.
DR InterPro; IPR002692; S45.
DR PANTHER; PTHR34218:SF4; ACYL-HOMOSERINE LACTONE ACYLASE QUIP; 1.
DR PANTHER; PTHR34218; PEPTIDASE S45 PENICILLIN AMIDASE; 1.
DR Pfam; PF13523; Acetyltransf_8; 1.
DR Pfam; PF01804; Penicil_amidase; 2.
DR SMART; SM01006; AlcB; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000199645}.
FT DOMAIN 615..663
FT /note="Acyltransferase MbtK/IucB-like conserved"
FT /evidence="ECO:0000259|SMART:SM01006"
SQ SEQUENCE 782 AA; 86044 MW; 99CC6074133D660B CRC64;
MKLYRDDHGI PHLRAGSVLD LAWLQGRVTA TDRGRQITVE RLRSEGRLAS VAGAAEVGWD
RFARRARLDD TAQRSFATLD ISTQRWLEAY TDGVRAGGIE WHPWSSLGVF QVQHILFGTF
GNKMWRAHVE RTLGPHALSW FAIEGPGGSG SNAWTVPGQI AGDPHRLLEL PGVYQQIRLA
CPDFDVAGLT FPGVPGVQHF GHAGSVAWAI TNAMADYQDL YIEELREAGG VLQARGATGW
EPVATHQETI VVRDDDPVVV DVIETARGPV IDGNLSLRTP ARSAFDLGFD ALLPLLHAST
VDDVADALSR WAEPVNSVLT ADSTGRALQL TVGRVPERDD RNRLVPVPAW EPRHDWKPDW
APMFRAEITT AVNANDRRPD TAPYGVDFAP PARARRIREL LDLGVPHERI HMDTALPAGS
ADAGRRMARQ AARARAVCER PELRPLFEPS GHDPLFAPWT DPRARIGIAL DGVLAGLGLD
LDPVLAEPLP DTPWGDRHLL YPLQLPGLNA VVPQIPLGGS AGCVLNTSSV PGVSDLCWRG
PVARYVWDLA DRGRSRWVVP FGASDDPASP HFLDQLPLWA SGELAPLVTD WELLTEEPVI
VFAEKLPGLG ELTMIRLDPA AHAPVVHSWV IKERNRFWGM GEHTVADVEE IYGFVDGLDS
HHAYLLLLDG GPIGVFQTYE PSQDPVGECY DVLPGDFGLH LLLDATGREL PHLTSAVFPA
LLRHLFAEPE RRRIIAEPDI RNERMISRLR REGFTLGPEI DLGHKKAQLT FLERDRFEGA
AA
//