ID AMPS_BACSU Reviewed; 410 AA.
AC P39762;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Aminopeptidase AmpS;
DE EC=3.4.11.-;
GN Name=ampS; OrderedLocusNames=BSU14450;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969500; DOI=10.1099/13500872-142-11-3033;
RA Winters P., Caldwell R.M., Enfield L., Ferrari E.;
RT "The ampS-nprE (124 degrees-127 degrees) region of the Bacillus subtilis
RT 168 chromosome: sequencing of a 27 kb segment and identification of several
RT genes in the area.";
RL Microbiology 142:3033-3037(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Caldwell R.M., Ferrari E.;
RT "Sequence analysis of the mobA-ampS region of the Bacillus subtilis
RT chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-291.
RC STRAIN=168 / JH642;
RA Kobayashi K., Sato T., Kobayashi Y.;
RT "The nucleotide sequence analysis of kinC region.";
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Metal-dependent exopeptidase. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:P42778};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P42778};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P42778};
CC Note=Binds 2 divalent metal cations per subunit. Can use cobalt, zinc,
CC and possibly also magnesium ions. {ECO:0000250|UniProtKB:P42778};
CC -!- SIMILARITY: Belongs to the peptidase M29 family. {ECO:0000305}.
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DR EMBL; AF012285; AAC24920.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13318.1; -; Genomic_DNA.
DR EMBL; D37799; BAA07046.1; -; Genomic_DNA.
DR PIR; C69585; C69585.
DR RefSeq; NP_389328.1; NC_000964.3.
DR RefSeq; WP_003232341.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P39762; -.
DR SMR; P39762; -.
DR IntAct; P39762; 1.
DR STRING; 224308.BSU14450; -.
DR MEROPS; M29.002; -.
DR PaxDb; 224308-BSU14450; -.
DR EnsemblBacteria; CAB13318; CAB13318; BSU_14450.
DR GeneID; 938756; -.
DR KEGG; bsu:BSU14450; -.
DR PATRIC; fig|224308.179.peg.1575; -.
DR eggNOG; COG2309; Bacteria.
DR InParanoid; P39762; -.
DR OrthoDB; 9803993at2; -.
DR PhylomeDB; P39762; -.
DR BioCyc; BSUB:BSU14450-MONOMER; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR InterPro; IPR035097; M29_N-terminal.
DR InterPro; IPR000787; Peptidase_M29.
DR PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR34448:SF3; AMINOPEPTIDASE AMPS; 1.
DR Pfam; PF02073; Peptidase_M29; 1.
DR PRINTS; PR00919; THERMOPTASE.
DR SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..410
FT /note="Aminopeptidase AmpS"
FT /id="PRO_0000079174"
FT BINDING 250
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P42778"
FT BINDING 316
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P42778"
FT BINDING 316
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P42778"
FT BINDING 340
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P42778"
FT BINDING 340
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P42778"
FT BINDING 345
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P42778"
FT BINDING 378
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P42778"
FT BINDING 380
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P42778"
SQ SEQUENCE 410 AA; 45798 MW; 90E6D9C61F97EB04 CRC64;
MDSFSQKLNT YAQLAVEVGV NVQKGQYVVV NASTDVRDFV RLIVKHAYEK GAKNVTVNWQ
DDEVAKLKYE LAPFEAFEEY PEWEAKGREE LAKNGAAFIS VVSSNPDLLK GIDSKRIAAF
QKAAGKALHT YRQYIQSDKV SWTVVGAASA GWAHKVFPGK SEEEAIHLLW EEIFKATRVN
EDNPVQAWIN HDQNLHEKVD HLNERHYAAL HYQAEGTDLT IKLPRKHVWA GAGSVNESGH
EFMANMPTEE VFTLPQKDGV DGVVSSTKPL SYGGNIIENF TLTFENGRIV DIKAEKGEDI
LKELVETDEG SHYLGEVALV PYDSPISQSN ILFYNTLFDE NASNHLAIGS AYAFNIEGGK
QMSREELVKE GLNESITHVD FMIGSKDMNI DGITADGKRE PIFRNGNWAF
//
