ID A0A2P1PQI2_9GAMM Unreviewed; 1415 AA.
AC A0A2P1PQI2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peptidase S8 {ECO:0008006|Google:ProtNLM};
GN ORFNames=C7S18_07675 {ECO:0000313|EMBL:AVP97078.1};
OS Ahniella affigens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Ahniella.
OX NCBI_TaxID=2021234 {ECO:0000313|EMBL:AVP97078.1, ECO:0000313|Proteomes:UP000241074};
RN [1] {ECO:0000313|EMBL:AVP97078.1, ECO:0000313|Proteomes:UP000241074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D13 {ECO:0000313|EMBL:AVP97078.1,
RC ECO:0000313|Proteomes:UP000241074};
RA Ko Y., Kim J.-H.;
RT "Ahniella affigens gen. nov., sp. nov., a gammaproteobacterium isolated
RT from sandy soil near a stream.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AVP97078.1, ECO:0000313|Proteomes:UP000241074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D13 {ECO:0000313|EMBL:AVP97078.1,
RC ECO:0000313|Proteomes:UP000241074};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP027860; AVP97078.1; -; Genomic_DNA.
DR KEGG; xba:C7S18_07675; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000241074; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02120; PA_subtilisin_like; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR045051; SBT.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF468; SUBTILISIN-LIKE PROTEASE SBT3.18; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000241074};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 162..194
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 221..657
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 459..545
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT ACT_SITE 230
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 297
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 622
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1415 AA; 148473 MW; 104A39BC542EE846 CRC64;
MARSWRCHCG RQRAKIRSAV MINRQQWRRL VVIAGLAVSP WVSFAATVEQ TPLAIGPTQK
AGASLADHAA KRHHTNRYLV ELKEPSAVAF RSLDQLGSIG KAIRLQPTAP EANGGQRFRA
DTPAVIAYRE YLHAAQDRAL SELSSTVGRT LASELRWDLI GNGFALTLSE SEAAALRDHP
LVQSVTRETV YQLQSDVGTR DIGADQVWTG TIPGSVLQTR GEGVVVGIVD SGINYGHPSF
ADLSPDGYNH TNPRGTRYGV CAGGTDPRCN DKLIGIYDFV NETGAQGASA GLDLGGHGTH
VAATAAGNPV SGQVTALSAS FPISATGVAP RANIIAYKAC GEGELSCPFA ATLAALNQAL
ADGVDVINFS LGGAAQSPWG DPRAFLDLRV AGTLAAVSAG NAGPINFTVG SPANAPWVVA
VANTYSSKRY TTVLGNINGT GITTPFSLGG QGISGGVAEA QVVYAGDFGD PTCTTSFPGG
TFTGRIVVCD NGRSDFSIQK SLRVASAGAV GLVIANREID GNGNAPNPFT TLPTVHVTFQ
DGQRLKTALR TARQGNGQIR ARIDGLNVQT GGAVGTLAES SSRGPVAPFS GYLKPNIAAP
GTNIVAAFQP SPTSFDVLTG TSMASPHIAG AIALLAAAHP DWTSDQLESA LLTTANATVL
KEDGLTPAAF YEGGAGMANI PAAMKAGLHF KVSKDAFLAS NPAAGGNPES LNMPYLHSEA
CVSRCTFDRT VTANVGGSWS IASTGNSGFS VQAEPNAISL TAGQSVTVRI TVSVTEPSAY
GRWLEGTLRF TSTTDPNGVS PTVVPVSVFA SGGASAFALN VTNANSAGAL TMNVPIAASL
AEATVKTTRM KAIVSANPVI PVDSTNDDAF DNTGQNFVRY VPLPTLGPEG NDGILYVDVR
PAATQDMDLF VGFDRNDNEI PEVDELLCAS TRSVGDADAC LVELPALSSS RPINYWIMVQ
NFSSAADNPA PEINVYTSTY LEVDSNLGGV AKAMLGRTNE RQELPIDFSW LLTDVAPGKK
AITVIRIGAD RNHAGNIVNI PVIVTRNTDA QLPPIVMNAR SDTKTLSLQP GQVHERIVVD
VPPNQTALVM RAEGIGGNVD LYVSKATAAP TPPVFAPAPP RNQQPFSSAT ASNNEVVALE
GSQLTAGRYY ITPVNSGTTV STVTLSVVGE FNSNTTRAPS NGYFNPGRSG HGLFLATLPN
LWAMAWYTFD FAGNPVWYTA QSSFVNETDS VWTANLFRST WNGSRDQPQL VGKVILTQTG
NGTFVFSWMV DGAYGSEPFQ PIGVPQCANG NFSVGGGWLR PDQSGWGSYF LNFAGNFEGE
ALYVYDDLGL PRWLIGDGTY APTLQKTFFQ VSGFCPTCAL VPTTRTSVGT ASRTLTTANQ
GSFTSNLTFR NNLTGTWVQN NVDWSKLTPD LSCAP
//
