ID A0A119CXD8_THIDE Unreviewed; 317 AA.
AC A0A119CXD8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Peptidase S49 {ECO:0000313|EMBL:KVW98011.1};
GN ORFNames=ABW22_03035 {ECO:0000313|EMBL:KVW98011.1};
OS Thiobacillus denitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW98011.1, ECO:0000313|Proteomes:UP000064243};
RN [1] {ECO:0000313|EMBL:KVW98011.1, ECO:0000313|Proteomes:UP000064243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RG {ECO:0000313|EMBL:KVW98011.1,
RC ECO:0000313|Proteomes:UP000064243};
RX PubMed=26712544;
RA Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, Subglacial
RT Chemoautotroph.";
RL Appl. Environ. Microbiol. 82:1486-1495(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:KVW98011.1}.
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; LDUG01000011; KVW98011.1; -; Genomic_DNA.
DR RefSeq; WP_059751851.1; NZ_LDUG01000011.1.
DR AlphaFoldDB; A0A119CXD8; -.
DR STRING; 1123392.GCA_000376425_02425; -.
DR PATRIC; fig|36861.3.peg.48; -.
DR OrthoDB; 9764363at2; -.
DR Proteomes; UP000064243; 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 Reference proteome {ECO:0000313|Proteomes:UP000064243};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 133..279
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
SQ SEQUENCE 317 AA; 34724 MW; 683C29C73DA7D976 CRC64;
MSEPEKSAPA NWERDVLEKL ALSAVQEQRR SRHWSILFKT LGFLYLFIVL FMVAGWFRSD
GVSLPKAHTA LIDIRGVISA DQTSSDSVIG SLQGAFEDKQ TRGVILRINS PGGSPVQAGQ
IYDEIKRLRA LHPKTPLYAV VDDICASGGY YVAVGADKIF VDKASIVGSI GVLMDGFGFT
ETMQKLGVER RLLTAGENKG FLDPFSPVDP EQQAFARQML EEIHGQFIAV VREGRGKRLK
ETPETFSGLV WSGEKSIQLG LADAYGSVES VARDVIKAKD IVDYTQRPGL AERLASRLGT
SMAKAWTPFE QAGATLR
//
