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Carboxypeptidase 1 (EC 3.4.17.19) (BsuCP)

 CBP1_BACSU              Reviewed;         501 AA.
P50848;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
07-JUN-2017, entry version 117.
RecName: Full=Carboxypeptidase 1;
EC=3.4.17.19 {ECO:0000269|PubMed:19544567};
AltName: Full=BsuCP;
Name=ypwA; OrderedLocusNames=BSU22080;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
NCIMB 3610 / VKM B-501;
PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
Serror P.;
"Sequence analysis of the Bacillus subtilis chromosome region between
the serA and kdg loci cloned in a yeast artificial chromosome.";
Microbiology 142:2005-2016(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
NCIMB 3610 / VKM B-501;
PubMed=8969496; DOI=10.1099/13500872-142-11-3005;
Capuano V., Galleron N., Pujic P., Sorokin A., Ehrlich S.D.;
"Organization of the Bacillus subtilis 168 chromosome between kdg and
the attachment site of the SP beta prophage: use of long accurate PCR
and yeast artificial chromosomes for sequencing.";
Microbiology 142:3005-3015(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[4]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH ZINC IONS,
CATALYTIC ACTIVITY, FUNCTION, COFACTOR, AND SUBUNIT.
STRAIN=168;
PubMed=19544567; DOI=10.1002/prot.22478;
Lee M.M., Isaza C.E., White J.D., Chen R.P., Liang G.F., He H.T.,
Chan S.I., Chan M.K.;
"Insight into the substrate length restriction of M32
carboxypeptidases: characterization of two distinct subfamilies.";
Proteins 77:647-657(2009).
-!- FUNCTION: Broad specificity carboxypetidase that releases amino
acids sequentially from the C-terminus, including neutral,
aromatic, polar and basic residues. Has lower activity with
substrates ending with His or Trp. {ECO:0000269|PubMed:19544567}.
-!- CATALYTIC ACTIVITY: Release of a C-terminal amino acid with broad
specificity, except for -Pro. {ECO:0000269|PubMed:19544567}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:19544567};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:19544567};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19544567}.
-!- SIMILARITY: Belongs to the peptidase M32 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L47838; AAB38482.1; -; Genomic_DNA.
EMBL; L77246; AAA96610.1; -; Genomic_DNA.
EMBL; AL009126; CAB14125.1; -; Genomic_DNA.
PIR; D69943; D69943.
RefSeq; NP_390090.1; NC_000964.3.
RefSeq; WP_004398513.1; NZ_JNCM01000036.1.
PDB; 3HQ2; X-ray; 2.90 A; A/B=1-501.
PDBsum; 3HQ2; -.
ProteinModelPortal; P50848; -.
SMR; P50848; -.
STRING; 224308.Bsubs1_010100012156; -.
MEROPS; M32.006; -.
PaxDb; P50848; -.
EnsemblBacteria; CAB14125; CAB14125; BSU22080.
GeneID; 939061; -.
KEGG; bsu:BSU22080; -.
PATRIC; fig|224308.179.peg.2412; -.
eggNOG; ENOG4105CTD; Bacteria.
eggNOG; COG2317; LUCA.
HOGENOM; HOG000040803; -.
InParanoid; P50848; -.
KO; K01299; -.
OMA; EFGHALY; -.
PhylomeDB; P50848; -.
BioCyc; BSUB:BSU22080-MONOMER; -.
EvolutionaryTrace; P50848; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
CDD; cd06460; M32_Taq; 1.
InterPro; IPR001333; Peptidase_M32_Taq.
Pfam; PF02074; Peptidase_M32; 1.
PIRSF; PIRSF006615; Zn_crbxpep_Taq; 1.
PRINTS; PR00998; CRBOXYPTASET.
1: Evidence at protein level;
3D-structure; Carboxypeptidase; Complete proteome; Hydrolase;
Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc.
CHAIN 1 501 Carboxypeptidase 1.
/FTId=PRO_0000078236.
ACT_SITE 266 266 Proton donor/acceptor. {ECO:0000250}.
METAL 265 265 Zinc; catalytic.
{ECO:0000269|PubMed:19544567}.
METAL 269 269 Zinc; catalytic.
{ECO:0000269|PubMed:19544567}.
METAL 295 295 Zinc; catalytic.
{ECO:0000269|PubMed:19544567}.
HELIX 6 31 {ECO:0000244|PDB:3HQ2}.
TURN 32 34 {ECO:0000244|PDB:3HQ2}.
HELIX 40 59 {ECO:0000244|PDB:3HQ2}.
HELIX 61 72 {ECO:0000244|PDB:3HQ2}.
HELIX 74 76 {ECO:0000244|PDB:3HQ2}.
HELIX 79 95 {ECO:0000244|PDB:3HQ2}.
HELIX 100 122 {ECO:0000244|PDB:3HQ2}.
HELIX 126 147 {ECO:0000244|PDB:3HQ2}.
HELIX 155 161 {ECO:0000244|PDB:3HQ2}.
HELIX 167 189 {ECO:0000244|PDB:3HQ2}.
TURN 198 200 {ECO:0000244|PDB:3HQ2}.
HELIX 206 219 {ECO:0000244|PDB:3HQ2}.
STRAND 229 231 {ECO:0000244|PDB:3HQ2}.
STRAND 237 241 {ECO:0000244|PDB:3HQ2}.
STRAND 244 249 {ECO:0000244|PDB:3HQ2}.
HELIX 257 273 {ECO:0000244|PDB:3HQ2}.
HELIX 278 280 {ECO:0000244|PDB:3HQ2}.
STRAND 283 287 {ECO:0000244|PDB:3HQ2}.
HELIX 291 302 {ECO:0000244|PDB:3HQ2}.
TURN 303 307 {ECO:0000244|PDB:3HQ2}.
HELIX 309 312 {ECO:0000244|PDB:3HQ2}.
TURN 313 315 {ECO:0000244|PDB:3HQ2}.
HELIX 316 322 {ECO:0000244|PDB:3HQ2}.
TURN 324 329 {ECO:0000244|PDB:3HQ2}.
HELIX 332 339 {ECO:0000244|PDB:3HQ2}.
HELIX 348 350 {ECO:0000244|PDB:3HQ2}.
TURN 353 355 {ECO:0000244|PDB:3HQ2}.
HELIX 356 371 {ECO:0000244|PDB:3HQ2}.
HELIX 377 379 {ECO:0000244|PDB:3HQ2}.
HELIX 380 392 {ECO:0000244|PDB:3HQ2}.
TURN 399 404 {ECO:0000244|PDB:3HQ2}.
TURN 408 412 {ECO:0000244|PDB:3HQ2}.
HELIX 418 437 {ECO:0000244|PDB:3HQ2}.
HELIX 441 447 {ECO:0000244|PDB:3HQ2}.
HELIX 451 460 {ECO:0000244|PDB:3HQ2}.
TURN 461 466 {ECO:0000244|PDB:3HQ2}.
HELIX 470 478 {ECO:0000244|PDB:3HQ2}.
STRAND 479 481 {ECO:0000244|PDB:3HQ2}.
HELIX 484 498 {ECO:0000244|PDB:3HQ2}.
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


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