ID A0A1E4JU49_9PROT Unreviewed; 312 AA.
AC A0A1E4JU49;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Peptidase S49 {ECO:0000313|EMBL:ODU30566.1};
GN ORFNames=ABS93_01825 {ECO:0000313|EMBL:ODU30566.1};
OS Thiobacillus sp. SCN 62-729.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=1660148 {ECO:0000313|EMBL:ODU30566.1, ECO:0000313|Proteomes:UP000094151};
RN [1] {ECO:0000313|EMBL:ODU30566.1, ECO:0000313|Proteomes:UP000094151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
CC -!- SIMILARITY: Belongs to the peptidase S49 family.
CC {ECO:0000256|ARBA:ARBA00008683}.
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:ODU30566.1}.
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DR EMBL; MEFL01000023; ODU30566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4JU49; -.
DR Proteomes; UP000094151; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd07023; S49_Sppa_N_C; 1.
DR Gene3D; 6.20.330.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR002142; Peptidase_S49.
DR InterPro; IPR047272; S49_SppA_C.
DR PANTHER; PTHR42987; PEPTIDASE S49; 1.
DR PANTHER; PTHR42987:SF4; PROTEASE SLR0021-RELATED; 1.
DR Pfam; PF01343; Peptidase_S49; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 129..274
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
SQ SEQUENCE 312 AA; 34009 MW; 4415DFDBD6B95E9B CRC64;
MSEPTPNWER EVLEKLALSA IQEQRRSRHW SILFKTLGFL YLFIVLFLAA GWFGSDGVSI
KEHTALVDLQ GEIASDKASA DTVIASLQSA FDDKKTKGVV LRINSPGGSP VQAGQIHDEI
KRLRGLHPDI PLYVVVDDIC ASGGYYVAVG ADKIFVDKAS IVGSIGVLMD GFGFTQTMQK
LGVERRLLTA GENKGFLDPF SPVDPKQEAY AKQMLEEIHG QFINVVREGR GKRLKETPEM
FSGLVWSGEK SIQLGLADGL GNVESVARDV IKAKDIVDFT QHEGLAERLA GRLGASMAKA
LTPFEKAGVT LH
//
