CBP1_BACSU
ID CBP1_BACSU Reviewed; 501 AA.
AC P50848;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Carboxypeptidase 1;
DE EC=3.4.17.19 {ECO:0000269|PubMed:19544567};
DE AltName: Full=BsuCP;
GN Name=ypwA; OrderedLocusNames=BSU22080;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA Serror P.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT serA and kdg loci cloned in a yeast artificial chromosome.";
RL Microbiology 142:2005-2016(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8969496; DOI=10.1099/13500872-142-11-3005;
RA Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D.;
RT "Organization of the Bacillus subtilis 168 chromosome between kdg and the
RT attachment site of the SP beta prophage: use of long accurate PCR and yeast
RT artificial chromosomes for sequencing.";
RL Microbiology 142:3005-3015(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH ZINC IONS, CATALYTIC
RP ACTIVITY, FUNCTION, COFACTOR, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=19544567; DOI=10.1002/prot.22478;
RA Lee M.M., Isaza C.E., White J.D., Chen R.P., Liang G.F., He H.T.,
RA Chan S.I., Chan M.K.;
RT "Insight into the substrate length restriction of M32 carboxypeptidases:
RT characterization of two distinct subfamilies.";
RL Proteins 77:647-657(2009).
CC -!- FUNCTION: Broad specificity carboxypetidase that releases amino acids
CC sequentially from the C-terminus, including neutral, aromatic, polar
CC and basic residues. Has lower activity with substrates ending with His
CC or Trp. {ECO:0000269|PubMed:19544567}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal amino acid with broad specificity,
CC except for -Pro.; EC=3.4.17.19;
CC Evidence={ECO:0000269|PubMed:19544567};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:19544567};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:19544567};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19544567}.
CC -!- SIMILARITY: Belongs to the peptidase M32 family. {ECO:0000305}.
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DR EMBL; L47838; AAB38482.1; -; Genomic_DNA.
DR EMBL; L77246; AAA96610.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14125.1; -; Genomic_DNA.
DR PIR; D69943; D69943.
DR RefSeq; NP_390090.1; NC_000964.3.
DR RefSeq; WP_004398513.1; NZ_JNCM01000036.1.
DR PDB; 3HQ2; X-ray; 2.90 A; A/B=1-501.
DR PDBsum; 3HQ2; -.
DR AlphaFoldDB; P50848; -.
DR SMR; P50848; -.
DR STRING; 224308.BSU22080; -.
DR MEROPS; M32.006; -.
DR jPOST; P50848; -.
DR PaxDb; P50848; -.
DR PRIDE; P50848; -.
DR EnsemblBacteria; CAB14125; CAB14125; BSU_22080.
DR GeneID; 939061; -.
DR KEGG; bsu:BSU22080; -.
DR PATRIC; fig|224308.179.peg.2412; -.
DR eggNOG; COG2317; Bacteria.
DR InParanoid; P50848; -.
DR OMA; EFGHALY; -.
DR PhylomeDB; P50848; -.
DR BioCyc; BSUB:BSU22080-MON; -.
DR EvolutionaryTrace; P50848; -.
DR Proteomes; UP000001570; Chromosome.
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 InterPro; IPR001333; Peptidase_M32_Taq.
DR PANTHER; PTHR34217; PTHR34217; 1.
DR Pfam; PF02074; Peptidase_M32; 1.
DR PIRSF; PIRSF006615; Zn_crbxpep_Taq; 1.
DR PRINTS; PR00998; CRBOXYPTASET.
PE 1: Evidence at protein level;
KW 3D-structure; Carboxypeptidase; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Zinc.
FT CHAIN 1..501
FT /note="Carboxypeptidase 1"
FT /id="PRO_0000078236"
FT ACT_SITE 266
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19544567"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19544567"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19544567"
FT HELIX 6..31
FT /evidence="ECO:0007829|PDB:3HQ2"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 40..59
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 79..95
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 100..122
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 126..147
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 155..161
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 167..189
FT /evidence="ECO:0007829|PDB:3HQ2"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:3HQ2"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3HQ2"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:3HQ2"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 257..273
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:3HQ2"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 291..302
FT /evidence="ECO:0007829|PDB:3HQ2"
FT TURN 303..307
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:3HQ2"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 316..322
FT /evidence="ECO:0007829|PDB:3HQ2"
FT TURN 324..329
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 332..339
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:3HQ2"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 356..371
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 380..392
FT /evidence="ECO:0007829|PDB:3HQ2"
FT TURN 399..404
FT /evidence="ECO:0007829|PDB:3HQ2"
FT TURN 408..412
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 418..437
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 441..447
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 451..460
FT /evidence="ECO:0007829|PDB:3HQ2"
FT TURN 461..466
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 470..478
FT /evidence="ECO:0007829|PDB:3HQ2"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:3HQ2"
FT HELIX 484..498
FT /evidence="ECO:0007829|PDB:3HQ2"
SQ SEQUENCE 501 AA; 58175 MW; A7489BABEFA38F82 CRC64;
MEIHTYEKEF FDLLKRISHY SEAVALMHWD SRTGAPKNGS EDRAESIGQL STDIFNIQTS
DRMKELIDVL YERFDDLSED TKKAVELAKK EYEENKKIPE AEYKEYVILC SKAETAWEEA
KGKSDFSLFS PYLEQLIEFN KRFITYWGYQ EHPYDALLDL FEPGVTVKVL DQLFAELKEA
IIPLVKQVTA SGNKPDTSFI TKAFPKEKQK ELSLYFLQEL GYDFDGGRLD ETVHPFATTL
NRGDVRVTTR YDEKDFRTAI FGTIHECGHA IYEQNIDEAL SGTNLSDGAS MGIHESQSLF
YENFIGRNKH FWTPYYKKIQ EASPVQFKDI SLDDFVRAIN ESKPSFIRVE ADELTYPLHI
IIRYEIEKAI FSNEVSVEDL PSLWNQKYQD YLGITPQTDA EGILQDVHWA GGDFGYFPSY
ALGYMYAAQL KQKMLEDLPE FDALLERGEF HPIKQWLTEK VHIHGKRKKP LDIIKDATGE
ELNVRYLIDY LSNKYSNLYL L
