ID   NYLC_KOCS2              Reviewed;         355 AA.
AC   Q1EPR4;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=6-aminohexanoate-oligomer endohydrolase {ECO:0000305};
DE            EC=3.5.1.117 {ECO:0000269|PubMed:17827307};
DE   AltName: Full=6-aminohexanoate oligomer hydrolase {ECO:0000303|PubMed:17827307};
DE   AltName: Full=Ahx endo-type-oligomer hydrolase {ECO:0000303|PubMed:17827307};
DE   AltName: Full=Nylon hydrolase {ECO:0000250|UniProtKB:Q1EPR5};
DE   AltName: Full=Nylonase {ECO:0000250|UniProtKB:Q1EPR5};
DE   Contains:
DE     RecName: Full=6-aminohexanoate-oligomer endohydrolase alpha subunit {ECO:0000305};
DE   Contains:
DE     RecName: Full=6-aminohexanoate-oligomer endohydrolase beta subunit {ECO:0000305};
GN   Name=nylC {ECO:0000303|PubMed:17827307};
OS   Kocuria sp. (strain KY2).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria;
OC   unclassified Kocuria.
OX   NCBI_TaxID=388923;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 267-276, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND PROTEOLYTIC
RP   PROCESSING.
RC   STRAIN=KY2;
RX   PubMed=17827307; DOI=10.1128/aem.00777-07;
RA   Yasuhira K., Tanaka Y., Shibata H., Kawashima Y., Ohara A., Kato D.,
RA   Takeo M., Negoro S.;
RT   "6-Aminohexanoate oligomer hydrolases from the alkalophilic bacteria
RT   Agromyces sp. strain KY5R and Kocuria sp. strain KY2.";
RL   Appl. Environ. Microbiol. 73:7099-7102(2007).
CC   -!- FUNCTION: Involved in the degradation of nylon-6 oligomers. Degrades
CC       cyclic and linear oligomers of 6-aminohexanoate (Ahx) with a degree of
CC       polymerization greater than three by an endo-type mode. Cannot use Ahx
CC       cyclic dimer or the Ahx linear dimer. {ECO:0000269|PubMed:17827307}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-x + [N-
CC         (6-aminohexanoyl)]x.; EC=3.5.1.117;
CC         Evidence={ECO:0000269|PubMed:17827307};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.44 mg/ml for Ahx cyclic-oligomer {ECO:0000269|PubMed:17827307};
CC         Note=kcat is 11.7 sec(-1) with Ahx cyclic-oligomer as substrate.
CC         {ECO:0000269|PubMed:17827307};
CC       pH dependence:
CC         Optimum pH is 7.0-8.5. {ECO:0000269|PubMed:17827307};
CC   -!- PATHWAY: Xenobiotic degradation; nylon-6 oligomer degradation.
CC       {ECO:0000269|PubMed:17827307}.
CC   -!- SUBUNIT: Heterotetramer composed of 4 alpha/beta heterodimers.
CC       {ECO:0000250|UniProtKB:Q1EPR5}.
CC   -!- PTM: Expressed as an inactive precursor that is cleaved
CC       autocatalytically at Asn266/Thr267 to generate an active enzyme
CC       composed of an alpha subunit and a beta subunit.
CC       {ECO:0000269|PubMed:17827307}.
CC   -!- SIMILARITY: Belongs to the peptidase S58 family. {ECO:0000305}.
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DR   EMBL; AB262080; BAE95770.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1EPR4; -.
DR   SMR; Q1EPR4; -.
DR   MEROPS; P01.102; -.
DR   BRENDA; 3.5.1.117; 10251.
DR   UniPathway; UPA00207; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019876; P:nylon catabolic process; IDA:UniProtKB.
DR   InterPro; IPR016117; ArgJ-like_dom_sf.
DR   InterPro; IPR005321; Peptidase_S58_DmpA.
DR   PANTHER; PTHR36512; PTHR36512; 1.
DR   Pfam; PF03576; Peptidase_S58; 1.
DR   SUPFAM; SSF56266; SSF56266; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Nylon degradation.
FT   CHAIN           1..266
FT                   /note="6-aminohexanoate-oligomer endohydrolase alpha
FT                   subunit"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000452356"
FT   CHAIN           267..355
FT                   /note="6-aminohexanoate-oligomer endohydrolase beta
FT                   subunit"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000452357"
FT   ACT_SITE        267
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q1EPR5"
SQ   SEQUENCE   355 AA;  36844 MW;  0C373E5BD3FA30C1 CRC64;
     MNTTPVHALT DIDGGIAVDP APRLAGPPVF GGPGNAAFDL VPVRSTGRET LRFDFPGVSV
     GSAHYEEGPT GATVIHIPAG ARTAVDARGG AVGLSGGYDF NHAICLAGGA SYGLEAGAGV
     SGALLERLEY RTGFAEAQLV SSAVIYDFSA RSTAVYPDKA LGRAALEFAV PGEFPQGRAG
     AGMSASAGKV DWDRTEITGQ GAAFRRLGDV RILAVVVPNP VGVIMDRAGG IVRGNYDAQT
     GVRRHPVFDY QEAFAEQLPP VTQAGNTTIS AIVTNVRMSP VELNQFAKQV HSSMHRGIQP
     FHTDMDGDTL FAVTTDEIDL PTTPGSSRGR LSVNATALGA IASEVMWDAV LEAAK