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Database: UniProt
Entry: R7BRH8_9FIRM
LinkDB: R7BRH8_9FIRM
Original site: R7BRH8_9FIRM 
ID   R7BRH8_9FIRM            Unreviewed;       376 AA.
AC   R7BRH8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Trypsin-like serine proteases typically periplasmic contain C-terminal PDZ domain {ECO:0000313|EMBL:CDD68390.1};
GN   ORFNames=BN674_01027 {ECO:0000313|EMBL:CDD68390.1};
OS   Firmicutes bacterium CAG:475.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263026 {ECO:0000313|EMBL:CDD68390.1, ECO:0000313|Proteomes:UP000018161};
RN   [1] {ECO:0000313|EMBL:CDD68390.1, ECO:0000313|Proteomes:UP000018161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:475 {ECO:0000313|Proteomes:UP000018161};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CDD68390.1}.
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DR   EMBL; CBHN010000025; CDD68390.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7BRH8; -.
DR   Proteomes; UP000018161; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR43019:SF23; PROTEASE DO-LIKE 5, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 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:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CDD68390.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CDD68390.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018161};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        36..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   376 AA;  40064 MW;  1EDFB9233E9DE917 CRC64;
     MDDFNNFFDD QRNPQPEHTP VYHTPSPKNN NKLGPVGILC VVLAVVMCVV VLVNVIVLAS
     LKQTIAEEYA ASISADMREQ YREAIDEALS GTNVVDDVTK AATEKALEAL KTNIGLVANA
     KSASVARLYM YKDANVNPST TSYNGIASGF LISDSTSDSK YRYLLTNAHC VRYEATKTSS
     SGYPFGMGRV TYEWASYGTI ICMFDGDTSN YYKLEIVAYG AYQGDHLDAE TNDPDIALLR
     VVGKVVGSSV VDAQPSNADH PSLTIATNDS QRGTMVALIG NPEGVGSTNS ISTGIISQTG
     ITISSWGSGK FVMTDAAVNG GNSGGPMIDI LGNVVGIVES KLVDESIDNM GFALSVSTIR
     DFVDSVSQSH NLNLTV
//
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