YSDC_BACSU
ID YSDC_BACSU Reviewed; 361 AA.
AC P94521; Q795W6;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Putative aminopeptidase YsdC;
DE EC=3.4.11.-;
GN Name=ysdC; OrderedLocusNames=BSU28820;
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=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
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 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH METAL ION, COFACTOR,
RP SUBUNIT, AND PUTATIVE FUNCTION.
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
CC -!- FUNCTION: Putative aminopeptidase.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:16021622};
CC -!- SUBUNIT: Homododecamer. {ECO:0000305|PubMed:16021622}.
CC -!- SIMILARITY: Belongs to the peptidase M42 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z75208; CAA99585.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14842.1; -; Genomic_DNA.
DR PIR; A69984; A69984.
DR RefSeq; NP_390760.1; NC_000964.3.
DR RefSeq; WP_003229495.1; NZ_JNCM01000036.1.
DR PDB; 1VHE; X-ray; 1.90 A; A=2-361.
DR PDBsum; 1VHE; -.
DR AlphaFoldDB; P94521; -.
DR SMR; P94521; -.
DR STRING; 224308.BSU28820; -.
DR jPOST; P94521; -.
DR PaxDb; P94521; -.
DR PRIDE; P94521; -.
DR DNASU; 936750; -.
DR EnsemblBacteria; CAB14842; CAB14842; BSU_28820.
DR GeneID; 936750; -.
DR KEGG; bsu:BSU28820; -.
DR PATRIC; fig|224308.179.peg.3130; -.
DR eggNOG; COG1363; Bacteria.
DR InParanoid; P94521; -.
DR OMA; YTLDNKA; -.
DR PhylomeDB; P94521; -.
DR BioCyc; BSUB:BSU28820-MON; -.
DR EvolutionaryTrace; P94521; -.
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 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome.
FT CHAIN 1..361
FT /note="Putative aminopeptidase YsdC"
FT /id="PRO_0000360205"
FT ACT_SITE 214
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 BINDING 182
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT BINDING 182
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT BINDING 325
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:1VHE"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:1VHE"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1VHE"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:1VHE"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:1VHE"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1VHE"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:1VHE"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:1VHE"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1VHE"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1VHE"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1VHE"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:1VHE"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1VHE"
FT TURN 126..130
FT /evidence="ECO:0007829|PDB:1VHE"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1VHE"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1VHE"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:1VHE"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:1VHE"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:1VHE"
FT HELIX 181..198
FT /evidence="ECO:0007829|PDB:1VHE"
FT STRAND 203..212
FT /evidence="ECO:0007829|PDB:1VHE"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:1VHE"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:1VHE"
FT STRAND 231..240
FT /evidence="ECO:0007829|PDB:1VHE"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:1VHE"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:1VHE"
FT HELIX 273..286
FT /evidence="ECO:0007829|PDB:1VHE"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:1VHE"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:1VHE"
FT STRAND 314..323
FT /evidence="ECO:0007829|PDB:1VHE"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:1VHE"
FT HELIX 333..349
FT /evidence="ECO:0007829|PDB:1VHE"
FT HELIX 352..359
FT /evidence="ECO:0007829|PDB:1VHE"
SQ SEQUENCE 361 AA; 39217 MW; 12377C8A4E2D9DDD CRC64;
MAKLDETLTM LKDLTDAKGI PGNEREVRQV MKSYIEPFAD EVTTDRLGSL IAKKTGAENG
PKIMIAGHLD EVGFMVTQIT DKGFIRFQTV GGWWAQVMLA QRVTIVTKKG EITGVIGSKP
PHILSPEARK KSVEIKDMFI DIGASSREEA LEWGVLPGDM IVPHFEFTVM NNEKFLLAKA
WDNRIGCAIA IDVLRNLQNT DHPNIVYGVG TVQEEVGLRG AKTAAHTIQP DIAFGVDVGI
AGDTPGISEK EAQSKMGKGP QIIVYDASMV SHKGLRDAVV ATAEEAGIPY QFDAIAGGGT
DSGAIHLTAN GVPALSITIA TRYIHTHAAM LHRDDYENAV KLITEVIKKL DRKTVDEITY
Q
