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Database: UniProt
Entry: A0A1E4HE24_9PSEU
LinkDB: A0A1E4HE24_9PSEU
Original site: A0A1E4HE24_9PSEU 
ID   A0A1E4HE24_9PSEU        Unreviewed;       398 AA.
AC   A0A1E4HE24;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:ODT94939.1};
GN   ORFNames=ABS81_32055 {ECO:0000313|EMBL:ODT94939.1};
OS   Pseudonocardia sp. SCN 72-86.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1660131 {ECO:0000313|EMBL:ODT94939.1, ECO:0000313|Proteomes:UP000094542};
RN   [1] {ECO:0000313|EMBL:ODT94939.1, ECO:0000313|Proteomes:UP000094542}
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:ODT94939.1}.
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DR   EMBL; MEFA01000388; ODT94939.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4HE24; -.
DR   Proteomes; UP000094542; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009403; P:toxin biosynthetic process; IEA:InterPro.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR003825; Colicin-V_CvpA.
DR   InterPro; IPR047680; MarP-like.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   NCBIfam; NF033740; MarP_fam_protase; 1.
DR   PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
DR   PANTHER; PTHR43019:SF36; SERINE PROTEASE RV3671C; 1.
DR   Pfam; PF02674; Colicin_V; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ODT94939.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000313|EMBL:ODT94939.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        29..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        59..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        100..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   398 AA;  41160 MW;  CF8B405D16424D28 CRC64;
     MSWVDVLVVL LAIVAGVSGW RHGMAVAFLS FVGVLGGAIL GVRLAPLIVS GIQSQHTRVI
     VSIVVVVLLV ALGETTGVFF GRRIRDRITG ERVLKVDSSL GALLQAFTVV VAAWLVALPL
     ASASFPGLAA SVRSSEVLQS VDSVMPSGAR ALPAELRQLL DDSGFPDVLS PFAQTPISAV
     GPPDPALARS QVVRDVGGSV LKVRGRAPSC QRQLEGTGFV VGPQRVMTNA HVVAGTNQTS
     VEVPGRNGRT RTLTATVVSY DAEVDVAVLA VPDLDAEPLQ FAPNAAKPGD DAIVLGYPLD
     GPYTATAAKV RDRIQLRGPD IYDSGTVTRD VYTIRATVRS GNSGGPMIAP DGQVLGVVFG
     AALDDSETGF VLTAEQVANA LNASGGLTRK VDTGTCAA
//
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