ID A0A0A2ER59_PORCN Unreviewed; 316 AA.
AC A0A0A2ER59;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Membrane protein {ECO:0000313|EMBL:KGN80197.1};
GN ORFNames=HQ35_05705 {ECO:0000313|EMBL:KGN80197.1};
OS Porphyromonas cangingivalis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=36874 {ECO:0000313|EMBL:KGN80197.1, ECO:0000313|Proteomes:UP000030125};
RN [1] {ECO:0000313|EMBL:KGN80197.1, ECO:0000313|Proteomes:UP000030125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-109 OH1386 {ECO:0000313|Proteomes:UP000030125};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas cangingivalis strain:COT-109_OH1386 Genome sequencing.";
RL Submitted (AUG-2014) 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:KGN80197.1}.
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DR EMBL; JQJD01000043; KGN80197.1; -; Genomic_DNA.
DR RefSeq; WP_036851687.1; NZ_JQJD01000043.1.
DR AlphaFoldDB; A0A0A2ER59; -.
DR STRING; 36874.HQ34_00405; -.
DR eggNOG; COG1073; Bacteria.
DR OrthoDB; 9777090at2; -.
DR Proteomes; UP000030125; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR43358; ALPHA/BETA-HYDROLASE; 1.
DR PANTHER; PTHR43358:SF4; ALPHA_BETA HYDROLASE FOLD-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030125};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 147..312
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 316 AA; 36282 MW; 5E49A943F28BE46D CRC64;
MRLKKIYRFV ALVIFLLIIG LGAFAWYMLD LTLAMTHRGQ DIEGSYREMR DRYPTLGSWI
DSLRNVSALR DTFITAKDGT KLHGYYVRAA VPTAKTAVIV HGYTDNAIRM MMIGEVYHRH
LHYNVLLPDL RHAGLSEGGH IQMGWLDRFD VARWVDETPS IFGDSARVVV HGISMGAATT
MMYSGEDPSE RVKVFVPDCG YTSVWDQFAY RLKVEYGLPT FPILNAADII CQWRYGWGFK
EASSLNQIVR CDRPMLFIHG AEDDYVPTEM AYRLYDMKPG IKELWIAPRS AHAVAYLDHP
QEYISRVKTF VDPYMQ
//
