YHFE_BACSU
ID YHFE_BACSU Reviewed; 346 AA.
AC O07603; Q796U6;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Putative aminopeptidase YhfE;
DE EC=3.4.11.-;
GN Name=yhfE; OrderedLocusNames=BSU10200;
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=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
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).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M42 family. {ECO:0000305}.
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DR EMBL; Y14083; CAA74526.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12860.1; -; Genomic_DNA.
DR PIR; C69830; C69830.
DR RefSeq; NP_388901.1; NC_000964.3.
DR RefSeq; WP_009966936.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O07603; -.
DR SMR; O07603; -.
DR STRING; 224308.BSU10200; -.
DR MEROPS; M42.A02; -.
DR PaxDb; O07603; -.
DR PRIDE; O07603; -.
DR EnsemblBacteria; CAB12860; CAB12860; BSU_10200.
DR GeneID; 936306; -.
DR KEGG; bsu:BSU10200; -.
DR PATRIC; fig|224308.179.peg.1096; -.
DR eggNOG; COG1363; Bacteria.
DR InParanoid; O07603; -.
DR OMA; HGMERTH; -.
DR PhylomeDB; O07603; -.
DR BioCyc; BSUB:BSU10200-MON; -.
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; 2.40.30.40; -; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome.
FT CHAIN 1..346
FT /note="Putative aminopeptidase YhfE"
FT /id="PRO_0000389625"
FT ACT_SITE 219
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 346 AA; 38736 MW; CF605C49FA6FBFEE CRC64;
MTSVRKTMEL IKELVSIPSP TGNTYEVINY IESLLKEWKV ETVRNHKGGL IATLPGRDTS
RHRMLTAHVD TLGAMVKEIK ADGRLKIDLI GGFRYNSIEG EYCQIETASG KMYTGTILMH
QTSVHVYKDA GKAERNQENM EIRLDEPVHC RKDTEELGIG VGDFVSFDPR VEITSSGFIK
SRHLDDKASV ALLLRLIHEI QTEDIELPYT THFLISNNEE IGYGGNSNIP PETVEYLAVD
MGAIGDGQAT DEYSVSICVK DASGPYHYQL RKHLVQLAEK HHIDYKLDIY PYYGSDASAA
IKSGHDIVHG LIGPGIDASH AFERTHKSSL RHTAKLLYYY VQSPMV
