BAPA_SPHMI
ID BAPA_SPHMI Reviewed; 396 AA.
AC A0MTQ2;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Beta-peptidyl aminopeptidase BapA {ECO:0000303|PubMed:17064315};
DE EC=3.4.11.25 {ECO:0000269|PubMed:17064315};
DE Contains:
DE RecName: Full=Beta-peptidyl aminopeptidase BapA alpha subunit {ECO:0000303|PubMed:17064315};
DE Contains:
DE RecName: Full=Beta-peptidyl aminopeptidase BapA beta subunit {ECO:0000303|PubMed:17064315};
DE Flags: Precursor;
OS Sphingosinicella microcystinivorans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingosinicellaceae; Sphingosinicella.
OX NCBI_TaxID=335406 {ECO:0000312|EMBL:ABK40073.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 19791 / CIP 109169 / JCM 13185 / KCTC 12019 / NCIMB 14270 / Y2
RC {ECO:0000312|EMBL:ABK40073.1};
RA Geueke B., Kohler H.-P.E.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17064315; DOI=10.1111/j.1742-4658.2006.05519.x;
RA Geueke B., Heck T., Limbach M., Nesatyy V., Seebach D., Kohler H.P.;
RT "Bacterial beta-peptidyl aminopeptidases with unique substrate
RT specificities for beta-oligopeptides and mixed beta,alpha-oligopeptides.";
RL FEBS J. 273:5261-5272(2006).
CC -!- FUNCTION: Beta-aminopeptidase that can cleave synthetic beta-peptides
CC which consist of backbone-elongated beta-amino acid residues that are
CC not processed by common proteolytic enzymes. Can cleave the beta-
CC peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-
CC homoLeu. Requires a beta-amino acid at the N-terminus of peptide
CC substrates and cleaves the peptide bond between the N-terminal beta-
CC amino acid and the amino acid at the second position of tripeptidic
CC substrates of the general structure H-betahXaa-Ile-betahTyr-OH
CC according to the following preferences with regard to the side chain of
CC the N-terminal beta-amino acid: aliphatic and aromatic > OH-containing
CC > hydrogen, basic and polar. beta-homoVal-beta-homoAla-beta-homoLeu and
CC beta-homoAla-beta-homoLeu. {ECO:0000269|PubMed:17064315}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves N-terminal beta-homoamino acids from peptides composed
CC of 2 to 6 amino acids.; EC=3.4.11.25;
CC Evidence={ECO:0000269|PubMed:17064315};
CC -!- ACTIVITY REGULATION: Inhibited by AEBSF (4-(2-
CC aminoethyl)benzenesulfonyl fluoride, Pefabloc SC).
CC {ECO:0000269|PubMed:17064315}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=39 mM for beta-homoVal-beta-homoAla-beta-homoLeu;
CC KM=41 mM for beta-homoAla-beta-homoLeu;
CC KM=4.4 mM for beta-3homoAla-pNA;
CC Vmax=0.84 umol/min/mg enzyme with beta-homoVal-beta-homoAla-beta-
CC homoLeu as substrate;
CC Vmax=3.1 umol/min/mg enzyme with beta-homoAla-beta-homoLeu as
CC substrate;
CC Vmax=0.063 umol/min/mg enzyme with carnosine as substrate
CC {ECO:0000269|PubMed:17064315};
CC Vmax=0.047 umol/min/mg enzyme with beta-homoGly-Ile-beta-homoTyr as
CC substrate {ECO:0000269|PubMed:17064315};
CC Vmax=0.45 umol/min/mg enzyme with beta-homoVal-Ile-beta-homoTyr as
CC substrate {ECO:0000269|PubMed:17064315};
CC Vmax=0.38 umol/min/mg enzyme with beta-homoVal-Ile-beta-homoTyr as
CC substrate {ECO:0000269|PubMed:17064315};
CC Vmax=0.46 umol/min/mg enzyme with beta-homoPhe-Ile-beta-homoTyr as
CC substrate {ECO:0000269|PubMed:17064315};
CC Vmax=0.21 umol/min/mg enzyme with beta-homoTyr-Ile-beta-homoTyr as
CC substrate {ECO:0000269|PubMed:17064315};
CC Vmax=0.040 umol/min/mg enzyme with beta-homoTrp-Ile-beta-homoTyr as
CC substrate {ECO:0000269|PubMed:17064315};
CC Vmax=0.40 umol/min/mg enzyme with beta-homoSer-Ile-beta-homoTyr as
CC substrate {ECO:0000269|PubMed:17064315};
CC Vmax=0.050 umol/min/mg enzyme with beta-homoThr-Ile-beta-homoTyr as
CC substrate {ECO:0000269|PubMed:17064315};
CC Vmax=0.011 umol/min/mg enzyme with beta-homoHis-Ile-beta-homoTyr as
CC substrate {ECO:0000269|PubMed:17064315};
CC Vmax=0.015 umol/min/mg enzyme with beta-homoLys-Ile-beta-homoTyr as
CC substrate {ECO:0000269|PubMed:17064315};
CC Vmax=0.011 umol/min/mg enzyme with beta-homoArg-Ile-beta-homoTyr as
CC substrate {ECO:0000269|PubMed:17064315};
CC Vmax=0.016 umol/min/mg enzyme with D-beta-homoVal-Ile-beta-homoTyr as
CC substrate {ECO:0000269|PubMed:17064315};
CC pH dependence:
CC Optimum pH is 10. {ECO:0000269|PubMed:17064315};
CC -!- SUBUNIT: Heterooctamer of 4 heterodimers ((alpha:beta)4); each
CC heterodimer is composed of an alpha subunit and a beta subunit
CC processed from the same precursor. {ECO:0000303|PubMed:17064315}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q52VH2}.
CC -!- PTM: Autoproteolytic processing to generate the alpha and beta subunit
CC is required for self-activation and is proposed to use a similar
CC mechanism as substrate cleavage. {ECO:0000250|UniProtKB:Q52VH2}.
CC -!- MISCELLANEOUS: S.microcystinivorans can degrade microcystin, a cyclic,
CC toxic heptapeptide that contains beta-peptidic substructures.
CC {ECO:0000303|PubMed:17064315}.
CC -!- SIMILARITY: Belongs to the peptidase S58 family. {ECO:0000305}.
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DR EMBL; EF043283; ABK40073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0MTQ2; -.
DR SMR; A0MTQ2; -.
DR MEROPS; P01.003; -.
DR BRENDA; 3.4.11.25; 12100.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Aminopeptidase; Hydrolase; Periplasm; Protease; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..270
FT /note="Beta-peptidyl aminopeptidase BapA alpha subunit"
FT /evidence="ECO:0000250|UniProtKB:Q52VH2"
FT /id="PRO_0000430765"
FT CHAIN 271..396
FT /note="Beta-peptidyl aminopeptidase BapA beta subunit"
FT /evidence="ECO:0000250|UniProtKB:Q52VH2"
FT /id="PRO_0000430766"
FT ACT_SITE 271
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q52VH2"
FT ACT_SITE 309
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q52VH2"
FT ACT_SITE 311
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q52VH2"
SQ SEQUENCE 396 AA; 41184 MW; 52E275E9E33A8C5C CRC64;
MHYLKFPAII AGMLLAGAAS AEGPRARDLG VPFAGKPGAN NAITDVAGVE VGYVSLISGE
GKLERGKGPV RTGVTAVLPR GKESRTPVYA GWETSNAAGE MTGTVWLEER GYFDGPMMIT
NTHSVGVVRD AVVGWLADVK WPGAWFTPVV AETYDGMLND INGFHVKPEH ALRAIQTAAS
GPVAEGNVGG GVGMQCFGFK GGTGTASRVV EMDGKSYTVG VLVQCNFGMR PWLRVAGAPV
GEELAGKYLP ETRGTQTAAA TNNGVAPGDG SIIVVMATDA PMLPHQLKRL AKRAAAGMGR
MGDAGSNGSG DIFVAFSTAN ANVQSVGGNV ISVETMPNDK LTLIFEAATQ ATEEAITNVL
VAADTLTGVN GYTIQRLPHA ELRAILKKYR RLAAAK
