CBPB_HELZE
ID CBPB_HELZE Reviewed; 429 AA.
AC Q3T905;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Carboxypeptidase B {ECO:0000303|PubMed:16260742};
DE Short=CPBHz {ECO:0000303|PubMed:16260742};
DE EC=3.4.17.2 {ECO:0000269|PubMed:16260742};
DE Flags: Precursor;
GN Name=CPB {ECO:0000303|PubMed:16260742};
OS Helicoverpa zea (Corn earworm moth) (Heliothis zea).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Helicoverpa.
OX NCBI_TaxID=7113 {ECO:0000312|EMBL:CAJ30028.1};
RN [1] {ECO:0000312|EMBL:CAJ30028.1, ECO:0007744|PDB:2C1C}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF
RP 117-428 IN COMPLEX WITH ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISULFIDE BOND.
RC TISSUE=Midgut {ECO:0000312|EMBL:CAJ30028.1};
RX PubMed=16260742; DOI=10.1073/pnas.0505489102;
RA Bayes A., Comellas-Bigler M., Rodriguez de la Vega M., Maskos K., Bode W.,
RA Aviles F.X., Jongsma M.A., Beekwilder J., Vendrell J.;
RT "Structural basis of the resistance of an insect carboxypeptidase to plant
RT protease inhibitors.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16602-16607(2005).
CC -!- FUNCTION: Metalloprotease which cleaves a single amino acid from the C-
CC terminal end of polypeptide chains. Shows a strong preference for
CC peptides with a terminal lysine residue. {ECO:0000269|PubMed:16260742}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential release of a C-terminal lysine or arginine amino
CC acid.; EC=3.4.17.2; Evidence={ECO:0000269|PubMed:16260742};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:16260742};
CC -!- ACTIVITY REGULATION: Highly resistant to inhibition by potato
CC carboxypeptidase inhibitor (PCI). Moderately inhibited by leech
CC carboxypeptidase inhibitor (LCI) and tick carboxypeptidase inhibitor
CC (TCI). {ECO:0000269|PubMed:16260742}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.26 mM for benzoyl-glycyl-lysine (Bz-Gly-Lys)
CC {ECO:0000269|PubMed:16260742};
CC KM=0.061 mM for N-(4-furylacryloyl)-Ala-Lys (FAAK)
CC {ECO:0000269|PubMed:16260742};
CC Note=kcat is 45.7 sec(-1) for benzoyl-glycyl-lysine (Bz-Gly-Lys).
CC kcat is 15.3 sec(-1) for N-(4-furylacryloyl)-Ala-Lys (FAAK).
CC {ECO:0000269|PubMed:16260742};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM085495; CAJ30028.1; -; mRNA.
DR PDB; 2C1C; X-ray; 2.30 A; A/B=117-428.
DR PDBsum; 2C1C; -.
DR AlphaFoldDB; Q3T905; -.
DR SMR; Q3T905; -.
DR BindingDB; Q3T905; -.
DR ChEMBL; CHEMBL6098; -.
DR MEROPS; M14.032; -.
DR BRENDA; 3.4.17.2; 2610.
DR EvolutionaryTrace; Q3T905; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR Gene3D; 3.30.70.340; -; 1.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF02244; Propep_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carboxypeptidase; Disulfide bond; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Secreted; Signal; Zinc.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..429
FT /note="Carboxypeptidase B"
FT /id="PRO_5012587721"
FT ACT_SITE 387
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT BINDING 182..185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16260742,
FT ECO:0007744|PDB:2C1C"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16260742,
FT ECO:0007744|PDB:2C1C"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 256..257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16260742,
FT ECO:0007744|PDB:2C1C"
FT BINDING 310..311
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT DISULFID 250..273
FT /evidence="ECO:0000269|PubMed:16260742,
FT ECO:0007744|PDB:2C1C"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:2C1C"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:2C1C"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:2C1C"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:2C1C"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:2C1C"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:2C1C"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:2C1C"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:2C1C"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:2C1C"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:2C1C"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:2C1C"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:2C1C"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:2C1C"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:2C1C"
FT HELIX 286..298
FT /evidence="ECO:0007829|PDB:2C1C"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:2C1C"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:2C1C"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:2C1C"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:2C1C"
FT HELIX 329..344
FT /evidence="ECO:0007829|PDB:2C1C"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:2C1C"
FT HELIX 359..363
FT /evidence="ECO:0007829|PDB:2C1C"
FT HELIX 371..377
FT /evidence="ECO:0007829|PDB:2C1C"
FT STRAND 381..387
FT /evidence="ECO:0007829|PDB:2C1C"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:2C1C"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:2C1C"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:2C1C"
FT HELIX 405..427
FT /evidence="ECO:0007829|PDB:2C1C"
SQ SEQUENCE 429 AA; 48393 MW; F69B14B8DAB14B6B CRC64;
MKFLLVLALC AVVYAKHEAY IGWKSYYVGV ATDAQAKALE PLIQKYELDF LSHPTKSREG
VVLVKPQHQA GFVQDIEAGG ITYRIHADDV KRQLEFDDQL IEMQRMSSFT RTAGRQLPYD
NYQELEVIDE YLDYIGEKYP DVATVVNAAE SFEGRPIKYI KISTTNFEDE NKPVIFIDGG
IHAREWISPP SVTWAIHKLV EDVTENDLLE KFDWILLPVV NPDGYKYTFT NERFWRKTRS
TNNNPLSQIC RGADGNRNFD FVWNSIGTSN SPCSDIYAGT SAFSEVETRV VRDILHEHLA
RMALYLTMHS FGSMILYPWG HDGSLSQNAL GLHTVGVAMA SVIQSNALPN FPPYTVGNSA
LVIGYYIAGS SEDYAHSIGV PLSYTYELPG LSSGWDGFHL PPQYIEQVCR ETWEGIVVGA
RRAGDLFRK
