ID D7GF94_PROFC Unreviewed; 420 AA.
AC D7GF94;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN Name=apeB {ECO:0000313|EMBL:CBL57205.1};
GN OrderedLocusNames=PFREUD_16940 {ECO:0000313|EMBL:CBL57205.1};
OS Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM
OS 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=754252 {ECO:0000313|EMBL:CBL57205.1, ECO:0000313|Proteomes:UP000000936};
RN [1] {ECO:0000313|EMBL:CBL57205.1, ECO:0000313|Proteomes:UP000000936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1
RC {ECO:0000313|Proteomes:UP000000936};
RX PubMed=20668525; DOI=10.1371/journal.pone.0011748;
RA Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S.,
RA Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P.,
RA Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., Gaillardin C.,
RA Lortal S.;
RT "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy
RT actinobacterium with food and probiotic applications.";
RL PLoS ONE 5:E11748-E11748(2010).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU004387};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR EMBL; FN806773; CBL57205.1; -; Genomic_DNA.
DR AlphaFoldDB; D7GF94; -.
DR STRING; 754252.PFREUD_16940; -.
DR KEGG; pfr:PFREUD_16940; -.
DR eggNOG; COG1362; Bacteria.
DR HOGENOM; CLU_019532_2_0_11; -.
DR Proteomes; UP000000936; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU004386};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW Reference proteome {ECO:0000313|Proteomes:UP000000936};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 420 AA; 45115 MW; 978FACA6BC8DC0AF CRC64;
MADPSEFMTA FAQFISSSPT SYHAAETMSA LLDRAGFEAM DEKLPWTGVA GRRYFVRGGA
VVAWIAPERV EPTTGFRIVG VHTDSPALKL KPEPVYDNAG WQQLNMEVYG GPLINSWLDR
ELGLAGRITT RTGENHLVRT GPIMRVSQLA PHLDRSVNQA LTVDQQYELM PSYGLGSEPD
VIELLCGQAG ILPTEFGFAD VYAYPTQEPA LFGNQSEFFA SSRLDNLSSV FPGLLALLRV
KSPHDVVVFS AFDHEEVGSS TTSGAAGPLL SDALTRIAAG LEVGGDAYQA MLARSSCISA
DAAHSVNPNH VSKYDPVVRP LMNQGPALKV NAKQRYATDS VTASLWLRAC EAAGVVHQSF
VSNNDVPCGT TIGPITATRL GIPTVDVGVP ILSMHSTREM CGSQDPQLLS RALEAYWMGA
//
