ID   AAC_ACTUT               Reviewed;         786 AA.
AC   P29958;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Aculeacin-A acylase;
DE            EC=3.5.1.-;
DE   Contains:
DE     RecName: Full=Aculeacin-A acylase small subunit;
DE   Contains:
DE     RecName: Full=Aculeacin-A acylase large subunit;
DE   Flags: Precursor;
GN   Name=aac;
OS   Actinoplanes utahensis.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Actinoplanes.
OX   NCBI_TaxID=1869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 35-53; 212-214
RP   AND 230-249.
RC   STRAIN=NRRL 12052;
RX   PubMed=1398088; DOI=10.1016/0378-1119(92)90063-u;
RA   Inokoshi J., Takeshima H., Ikeda H., Omura S.;
RT   "Cloning and sequencing of the aculeacin A acylase-encoding gene from
RT   Actinoplanes utahensis and expression in Streptomyces lividans.";
RL   Gene 119:29-35(1992).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the palmitoyl moiety of the
CC       antifungal antibiotic, aculeacin-A, giving a hexapeptide moiety and a
CC       long chain fatty acid.
CC   -!- SUBUNIT: Heterodimer of a small subunit and a large subunit processed
CC       from the same precursor.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S45 family. {ECO:0000305}.
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DR   EMBL; D10610; BAA01465.1; -; Genomic_DNA.
DR   PIR; JC1298; JC1298.
DR   AlphaFoldDB; P29958; -.
DR   SMR; P29958; -.
DR   STRING; 1869.MB27_08700; -.
DR   MEROPS; S45.005; -.
DR   eggNOG; COG2366; Bacteria.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Gene3D; 1.10.1400.10; -; 1.
DR   Gene3D; 1.10.439.10; -; 1.
DR   Gene3D; 2.30.120.10; -; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR043147; Penicillin_amidase_A-knob.
DR   InterPro; IPR023343; Penicillin_amidase_dom1.
DR   InterPro; IPR043146; Penicillin_amidase_N_B-knob.
DR   InterPro; IPR002692; S45.
DR   PANTHER; PTHR34218; PTHR34218; 1.
DR   Pfam; PF01804; Penicil_amidase; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Secreted; Signal; Zymogen.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..34
FT                   /evidence="ECO:0000269|PubMed:1398088"
FT                   /id="PRO_0000020598"
FT   CHAIN           35..786
FT                   /note="Aculeacin-A acylase"
FT                   /id="PRO_0000253350"
FT   CHAIN           35..214
FT                   /note="Aculeacin-A acylase small subunit"
FT                   /id="PRO_0000020599"
FT   PROPEP          215..229
FT                   /note="Spacer peptide"
FT                   /evidence="ECO:0000269|PubMed:1398088"
FT                   /id="PRO_0000020600"
FT   CHAIN           230..786
FT                   /note="Aculeacin-A acylase large subunit"
FT                   /id="PRO_0000020601"
FT   REGION          35..130
FT                   /note="Substrate-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          220..239
FT                   /note="Possible recognition-sequence of an AAC processing
FT                   enzyme"
FT   REGION          658..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..688
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        230
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   786 AA;  84090 MW;  721D8A9D71E4C38C CRC64;
     MTSSYMRLKA AAIAFGVIVA TAAVPSPASG REHDGGYAAL IRRASYGVPH ITADDFGSLG
     FGVGYVQAED NICVIAESVV TANGERSRWF GATGPDDADV RTTSSTQAID DRVAERLLEG
     PRDGVRAPCD DVRDQMRGFV AGYNHFLRRT GVHRLTDPAC RGKAWVRPLS EIDLWRTSWD
     SMVRAGSGAL LDGIVAATPP TAAGPASAPE APDAAAIAAA LDGTSAGIGS NAYGLGAQAT
     VNGSGMVLAN PHFPWQGAER FYRMHLKVPG RYDVEGAALI GDPIIEIGHN RTVAWSHTVS
     TARRFVWHRL SLVPGDPTSY YVDGRPERMR ARTVTVQTGS GPVSRTFHDT RYGPVAVVPG
     TFDWTPATAY AITDVNAGNN RAFDGWLRMG QAKDVRALKA VLDRHQFLPW VNVIAADARG
     EALYGDHSVV PRVTGALAAA CIPAPFQPLY ASSGQAVLDG SRSDCALGAD PDAAVPGILG
     PASLPVRFRD DYVTNSNDSH WLASPAAPLE GFPRILGNER TPRSLRTRLG LDQIQQRLAG
     TDGLPGKGFT TARLWQVMFG NRMHGAELVR DDLVALCRRQ PTATASNGAI VDLTAACTAL
     SRFDERADLD SRGAHLFTEF LAGGIRFADT FEVTDPVRTP APFWNTTDPR VRTALADACN
     GSPASPSTRS VGDIHTDSRG ERRIPIHGGR GEAGTFNVIT NPLVPGVGYP QVVHGTSFVM
     AVELGPHGPS GRQILTYAQS TNPNSPWYAD QTVLYSRKGW DTIKYTEAQI AADPNLRVYR
     VAQRGR