ID   A0A254THI0_9BURK        Unreviewed;       335 AA.
AC   A0A254THI0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Peptidase S49 {ECO:0000313|EMBL:OWW22100.1};
GN   ORFNames=AYR66_24005 {ECO:0000313|EMBL:OWW22100.1};
OS   Noviherbaspirillum denitrificans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Noviherbaspirillum.
OX   NCBI_TaxID=1968433 {ECO:0000313|EMBL:OWW22100.1, ECO:0000313|Proteomes:UP000197535};
RN   [1] {ECO:0000313|EMBL:OWW22100.1, ECO:0000313|Proteomes:UP000197535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSA40 {ECO:0000313|EMBL:OWW22100.1,
RC   ECO:0000313|Proteomes:UP000197535};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:OWW22100.1}.
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; LSTO01000001; OWW22100.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A254THI0; -.
DR   OrthoDB; 9764363at2; -.
DR   Proteomes; UP000197535; 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   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:UP000197535};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          149..288
FT                   /note="Peptidase S49"
FT                   /evidence="ECO:0000259|Pfam:PF01343"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   335 AA;  36631 MW;  B27116FAAA159556 CRC64;
     MIEDNFEEQN QIRTSVPPSA SHQGTGWERE VLEKLAFATL REQRAARRWN IFFRIVTLSL
     IGFGMWLAFG YTQQDAEVVG PHTALIEIDG TIESGTSGSA DAVIQALNRA YSDESSVGVV
     LRINSPGGSP VQAGMINDEI GRLRQEFPKK PLYVVVDEIC ASGGYYIAAA ADKIFVNKAS
     IVGSIGVLMD GFGFTGLMDK AGIERRLMTA GENKGFLDPF SPQSAKHRNY AQDMLNEVHQ
     QFIDVVRHGR GDRLKETPET FSGLFWSGSK AVEIGLADGF GTVDSVARDE LKAEDIVDYT
     QREGLSERLL KKFGGAVGTA VVNSLWTTSA RPAFR
//