BSAP_BACSU
ID BSAP_BACSU Reviewed; 455 AA.
AC P25152;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Aminopeptidase YwaD;
DE AltName: Full=Arginyl aminopeptidase;
DE EC=3.4.11.6;
DE AltName: Full=BSAP;
DE AltName: Full=Leucyl aminopeptidase;
DE EC=3.4.11.10;
DE Flags: Precursor;
GN Name=ywaD; OrderedLocusNames=BSU38470; ORFNames=ipa-8r;
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;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
RC STRAIN=168;
RX PubMed=1806041; DOI=10.3109/10425179109020780;
RA Glaser P., Kunst F., Debarbouille M., Vertes A., Danchin A., Dedonder R.;
RT "A gene encoding a tyrosine tRNA synthetase is located near sacS in
RT Bacillus subtilis.";
RL DNA Seq. 1:251-261(1991).
RN [4]
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=15583392; DOI=10.1107/s0907444904026976;
RA Reiland V., Fundoiano-Hershcovitz Y., Golan G., Gilboa R., Shoham Y.,
RA Shoham G.;
RT "Preliminary crystallographic characterization of BSAP, an extracellular
RT aminopeptidase from Bacillus subtilis.";
RL Acta Crystallogr. D 60:2371-2376(2004).
RN [5]
RP CATALYTIC ACTIVITY, FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=168 / BR151;
RX PubMed=15668014; DOI=10.1016/j.femsle.2004.12.001;
RA Fundoiano-Hershcovitz Y., Rabinovitch L., Shulami S., Reiland V.,
RA Shoham G., Shoham Y.;
RT "The ywad gene from Bacillus subtilis encodes a double-zinc
RT aminopeptidase.";
RL FEMS Microbiol. Lett. 243:157-163(2005).
CC -!- FUNCTION: Catalyzes the hydrolysis of a range of N-terminal amino
CC acids. {ECO:0000269|PubMed:15668014}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal Arg and Lys from oligopeptides when P1'
CC is not Pro. Also acts on arylamides of Arg and Lys.; EC=3.4.11.6;
CC Evidence={ECO:0000269|PubMed:15668014};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, preferentially leucine,
CC but not glutamic or aspartic acids.; EC=3.4.11.10;
CC Evidence={ECO:0000269|PubMed:15668014};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15668014};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:15668014};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 mM for Arg-pNA {ECO:0000269|PubMed:15668014};
CC KM=0.85 mM for Lys-pNA {ECO:0000269|PubMed:15668014};
CC KM=3.6 mM for Leu-pNA {ECO:0000269|PubMed:15668014};
CC KM=19 mM for Val-pNA {ECO:0000269|PubMed:15668014};
CC KM=10 mM for Ala-pNA {ECO:0000269|PubMed:15668014};
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:15668014};
CC Temperature dependence:
CC Stable for 20 min at temperatures of up to 80 degrees Celsius.
CC {ECO:0000269|PubMed:15668014};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15583392}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
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DR EMBL; X73124; CAA51564.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15873.1; -; Genomic_DNA.
DR EMBL; X52480; CAA36725.1; -; Genomic_DNA.
DR PIR; S39663; S39663.
DR RefSeq; NP_391726.1; NC_000964.3.
DR RefSeq; WP_003242515.1; NZ_JNCM01000034.1.
DR PDB; 6HC6; X-ray; 1.77 A; A/B/C=1-455.
DR PDB; 6HC7; X-ray; 2.50 A; A/B/C=1-455.
DR PDBsum; 6HC6; -.
DR PDBsum; 6HC7; -.
DR AlphaFoldDB; P25152; -.
DR SMR; P25152; -.
DR STRING; 224308.BSU38470; -.
DR MEROPS; M28.009; -.
DR PaxDb; P25152; -.
DR PRIDE; P25152; -.
DR DNASU; 937350; -.
DR EnsemblBacteria; CAB15873; CAB15873; BSU_38470.
DR GeneID; 937350; -.
DR KEGG; bsu:BSU38470; -.
DR PATRIC; fig|224308.179.peg.4164; -.
DR eggNOG; COG2234; Bacteria.
DR InParanoid; P25152; -.
DR OMA; EPWYHTP; -.
DR BioCyc; BSUB:BSU38470-MON; -.
DR BRENDA; 3.4.11.10; 658.
DR BRENDA; 3.4.11.6; 658.
DR SABIO-RK; P25152; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..455
FT /note="Aminopeptidase YwaD"
FT /id="PRO_0000026854"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT HELIX 45..56
FT /evidence="ECO:0007829|PDB:6HC6"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:6HC6"
FT HELIX 67..82
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:6HC6"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6HC6"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:6HC6"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:6HC6"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 213..222
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:6HC6"
FT TURN 260..263
FT /evidence="ECO:0007829|PDB:6HC6"
FT HELIX 264..277
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 283..292
FT /evidence="ECO:0007829|PDB:6HC6"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:6HC6"
FT HELIX 299..306
FT /evidence="ECO:0007829|PDB:6HC6"
FT HELIX 310..315
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:6HC6"
FT HELIX 346..358
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:6HC6"
FT HELIX 373..378
FT /evidence="ECO:0007829|PDB:6HC6"
FT STRAND 382..389
FT /evidence="ECO:0007829|PDB:6HC6"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:6HC6"
FT TURN 398..401
FT /evidence="ECO:0007829|PDB:6HC6"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:6HC6"
FT HELIX 412..430
FT /evidence="ECO:0007829|PDB:6HC6"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:6HC6"
SQ SEQUENCE 455 AA; 49450 MW; 89EE6A6EEB0CCE18 CRC64;
MKKLLTVMTM AVLTAGTLLL PAQSVTPAAH AVQISNSERE LPFKAKHAYS TISQLSEAIG
PRIAGTAAEK KSALLIASSM RKLKLDVKVQ RFNIPDRLEG TLSSAGRDIL LQAASGSAPT
EEQGLTAPLY NAGLGYQKDF TADAKGKIAL ISRGDLTYYE KAKNAEAAGA KAVIIYNNKE
SLVPMTPNLS GNKVGIPVVG IKKEDGEALT QQKEATLKLK AFTNQTSQNI IGIKKPKNIK
HPDIVYVTAH YDSVPFSPGA NDNGSGTSVM LEMARVLKSV PSDKEIRFIA FGAEELGLLG
SSHYVDHLSE KELKRSEVNF NLDMVGTSWE KASELYVNTL DGQSNYVWES SRTAAEKIGF
DSLSLTQGGS SDHVPFHEAG IDSANFIWGD PETEEVEPWY HTPEDSIEHI SKERLQQAGD
LVTAAVYEAV KKEKKPKTIK KQMKAKASDI FEDIK
