ID A9D167_9GAMM Unreviewed; 740 AA.
AC A9D167;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Peptidase S46 {ECO:0008006|Google:ProtNLM};
GN ORFNames=KT99_08593 {ECO:0000313|EMBL:EDQ01952.1};
OS Shewanella benthica KT99.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=314608 {ECO:0000313|EMBL:EDQ01952.1, ECO:0000313|Proteomes:UP000005839};
RN [1] {ECO:0000313|EMBL:EDQ01952.1, ECO:0000313|Proteomes:UP000005839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT99 {ECO:0000313|EMBL:EDQ01952.1,
RC ECO:0000313|Proteomes:UP000005839};
RA Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S46 family.
CC {ECO:0000256|ARBA:ARBA00010491}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDQ01952.1}.
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DR EMBL; ABIC01000006; EDQ01952.1; -; Genomic_DNA.
DR RefSeq; WP_005497287.1; NZ_ABIC01000006.1.
DR AlphaFoldDB; A9D167; -.
DR STRING; 314608.KT99_08593; -.
DR MEROPS; S46.003; -.
DR Proteomes; UP000005839; Unassembled WGS sequence.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:InterPro.
DR GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:InterPro.
DR GO; GO:1901565; P:organonitrogen compound catabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR019500; Pep_S46.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000126; V8_ser_AS.
DR PANTHER; PTHR38469; -; 1.
DR PANTHER; PTHR38469:SF1; PERIPLASMIC PEPTIDASE SUBFAMILY S1B; 1.
DR Pfam; PF10459; Peptidase_S46; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00673; V8_SER; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022438};
KW Protease {ECO:0000256|ARBA:ARBA00022438}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..740
FT /note="Peptidase S46"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002737106"
SQ SEQUENCE 740 AA; 83023 MW; 34CF6B5EAFE9C9EA CRC64;
MRNALISALV LSSGVAFISL ETHADEGQWQ PYQMPSIADK LSERGISIPA TQLADLTQYP
MNAVVGLGYC TASFVSPQGL VVTNHHCAYR AIQYNSKKEH NYIADGFLAT SKIDEPSAGP
NERLYITEAV TNVSEQVTQD LSQDPLVRYE EIQSNRKSLI KSCESDDNYR CSVKSFHSGL
EYYLIKQLII RDVRLVYAPP KSVGAFGGDI DNYEYPRHAG DFTFLRAYVG KDGQPAAYAK
DNVPFKPKSY LKINADGVKA GDGVFVAGYP GSTSRYRLTS ELKFASDWLY PTLASRYQLR
IDTIEAMGDS SSEIEIKYAG TLASMANRMK KYNGLLDGFK ATDIAGIKQS REDDFKQWLA
TDKTYQSYQA QLDRLERLLS KKRIESQTRY YFENAQSSTL LAAANKLYRL SKEKTKPDAE
REEGYQERDM KMFKARLKRI DASFDTSVDK ALWLQDLQAY KAQDNRVAAL DAMLIDNQES
ASLSEKLDGL YSLTSLTNQD KRLAWMDAEA DAFETSADPF IRLAVALFDT NMAQEKDKKT
LAGELSQARP DYMKAIIAYY QANDWPVYPD ANGTLRISYG MVDGYQAKDA LYKQPFTHLE
GIAAKHTGVA PFNAPQKVLD AIKEQRYGSH KVASVINDPS TWLCRLFSCL DKPEAFNSVP
VNFLSSVDTT GGNSGSPVFN GKGELVGLNF DSTYEAITKD WFFNPSITRA IHVDFRYILW
MMDEVDHADN LIAELDLVRN
//
