ID A0A1Q2CG86_9ACTN Unreviewed; 558 AA.
AC A0A1Q2CG86;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Protease-4 {ECO:0000313|EMBL:SDY55612.1};
GN ORFNames=RPIT_10270 {ECO:0000313|EMBL:AQP45129.1}, SAMN05428934_102251
GN {ECO:0000313|EMBL:SDY55612.1};
OS Tessaracoccus flavus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1610493 {ECO:0000313|EMBL:AQP45129.1, ECO:0000313|Proteomes:UP000188324};
RN [1] {ECO:0000313|EMBL:AQP45129.1, ECO:0000313|Proteomes:UP000188324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RP1T {ECO:0000313|EMBL:AQP45129.1,
RC ECO:0000313|Proteomes:UP000188324};
RX PubMed=26869509; DOI=10.1099/ijsem.0.000958;
RA Kumari R., Singh P., Schumann P., Lal R.;
RT "Tessaracoccus flavus sp. nov., isolated from the drainage system of a
RT lindane-producing factory.";
RL Int. J. Syst. Evol. Microbiol. 66:1862-1868(2016).
RN [2] {ECO:0000313|EMBL:SDY55612.1, ECO:0000313|Proteomes:UP000199635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RP1 {ECO:0000313|EMBL:SDY55612.1,
RC ECO:0000313|Proteomes:UP000199635};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AQP45129.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RP1T {ECO:0000313|EMBL:AQP45129.1};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S49 family.
CC {ECO:0000256|ARBA:ARBA00008683}.
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DR EMBL; CP019605; AQP45129.1; -; Genomic_DNA.
DR EMBL; FNPU01000002; SDY55612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2CG86; -.
DR STRING; 1610493.RPIT_10270; -.
DR KEGG; tfl:RPIT_10270; -.
DR OrthoDB; 9764363at2; -.
DR Proteomes; UP000188324; Chromosome.
DR Proteomes; UP000199635; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd07018; S49_SppA_67K_type; 1.
DR CDD; cd07023; S49_Sppa_N_C; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR004634; Pept_S49_pIV.
DR InterPro; IPR002142; Peptidase_S49.
DR InterPro; IPR047217; S49_SppA_67K_type_N.
DR InterPro; IPR047272; S49_SppA_C.
DR PANTHER; PTHR33209; PROTEASE 4; 1.
DR PANTHER; PTHR33209:SF1; SERINE PROTEASE SPPA, CHLOROPLASTIC; 1.
DR Pfam; PF01343; Peptidase_S49; 2.
DR PIRSF; PIRSF001217; Protease_4_SppA; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SDY55612.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000188324};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 110..239
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 342..493
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT ACT_SITE 161
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
FT ACT_SITE 359
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ SEQUENCE 558 AA; 59523 MW; 7DCE005A7E848A48 CRC64;
MGLKDLLGKI TGDTPVVLEL DMARGVLVAK PTNPLQAVQL INSPTLNALR SHLREASRDA
RVLGLIVHAV PSGTALAYVE EIAGLIEDFG ESKKTMAWSE SFGELGQGLG AYRLAAAAQQ
IWLQPTGAVN IEGVEVSMTL LKGLFNKAGA EPQFGQRHEY KTAADTYAAD HVTEANREMT
SRLGQSIVEE FVAAVARLRS IPPERVWDGV NGSPLTAEQA LELGLIDRVG YRDEAYAATL
EEWGAEADHL LFAHRYTNKA AMAKKLAPKQ PKVAVVTLRG AIVTGRGQRS PMGGDQSGSD
VVDEHLRAAL RDEDVKAVVF EVDSPGGSAV ASDFIRRSVL RLREAGKPVV AHMGAVAASG
GYYVAMPCDE IVAEPSTLTG SIGVLAGKVV TRGTYDKLGL VRETIPVGAA AGMLSSAHEF
SDDDWDRLNR WLDRVYLDFT TFAAQDRGMD HDHLESLARG RVWTGADARD RGLVDHLGGQ
WLAVERACAL AGLDERRTKL THIGDAGLLT LLKPATSTEG AVGGANLPDA EGVLTALAAR
VGLHGRGALT MPWGLRIS
//