ID A0A0Q5HAF1_9BURK Unreviewed; 1065 AA.
AC A0A0Q5HAF1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASF77_09170 {ECO:0000313|EMBL:KQQ88878.1};
OS Massilia sp. Leaf139.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ88878.1, ECO:0000313|Proteomes:UP000051760};
RN [1] {ECO:0000313|EMBL:KQQ88878.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ88878.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ88878.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ88878.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KQQ88878.1}.
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DR EMBL; LMOJ01000022; KQQ88878.1; -; Genomic_DNA.
DR RefSeq; WP_056339218.1; NZ_LMOJ01000022.1.
DR AlphaFoldDB; A0A0Q5HAF1; -.
DR STRING; 1736272.ASF77_09170; -.
DR OrthoDB; 614750at2; -.
DR Proteomes; UP000051760; Unassembled WGS sequence.
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 CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 2.60.40.2310; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR046450; PA_dom_sf.
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; IPR034197; Peptidases_S8_3.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR045051; SBT.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF468; SUBTILISIN-LIKE PROTEASE SBT3.18; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
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:UP000051760};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1065
FT /note="Peptidase S8 and S53 subtilisin kexin sedolisin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006251311"
FT DOMAIN 32..132
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 161..662
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 459..534
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 730..821
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 170
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 269
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 624
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1065 AA; 109364 MW; 1E0CBEA067C99DC5 CRC64;
MKHSLRPISF AVMLMLAGVA ASTSAQETRR PYIVQLQDAP AATYVGGVEG LAPTQPAPGV
AFDYRAPQVQ DYVRYLGDRK SAVLATIGGA EIIADYDVVL NGFAVMLTDA QVLALKSNPD
VADVQADAAR KVDTISTSRF LGLSATGGLW SQYGQGSLVK GEGMVVGIVD SGIWPEDPAF
SDRVDADGKP TTDQSGTLAY AGRPASYTGY CQAGEGFDPV KHCNNKLIGA RYYNAGYLSA
RLPTNWSEYM SPRDSSNGTD GISFGHGGHG SHTASTAAGN AGTPVTIGGV KMGESSGMAP
RARIAAYKVC WTYDNPAAID GTNASNTCYN SDSVKAIDDA VKDGVNVINY SISGSQTSVA
DPVEQAFYRA SLANVFVAAS AGNSGPANAV AHISPWLTTV AASTHDRKFQ ADVVLGNGNR
YFGASYSEIP LPQTALIRAE DAGMGGSSAA DLCYSDAAAA AANNPGRPQV ILDPAKVAGK
IVICTRGNNA RVDKSLAVKQ AGGVGMILVD NGAGLVSEVH SVPTIHVSAA DGALIKAYAA
AQAANATSSL SAFYAGTKPA PIMAGFSSRG PNQGDSNILK PDLTAPGVDI IASVTATLTP
AQHAAVAAGT LVPPPAYESY QGTSMSSPHV AGLALLLRQQ HPDWSPAAIK SALMTTAYST
LNDGLAGAQN GLLPWSQGAG HVNPNKATNP GLVYDAGKAD YVAYQCKVNR AAVSPASDCT
TFGVLDETYN LNLPSITVGS IQGNVTVRRT VTNVSGTTAT FTPSGSMQGF SMSVSPASLT
LAPGAKGSFT LKLTATTAPA DEWKFGHLTW TGAGATVRSP IQARVGRPIT APVELTSDRV
SGSKLFGVKT GYSGRMGYIK GGLKDVTMGA PETLTPSQIN SASLKTICAA GASTDSVKVY
DVAVPAKAMV ARFALRQADV GSAADDHDLG LLSPDGTWTY SGNDGSGEAV QVVGPAAGNY
KVCVVAFGTS PKDAAMTHKL SSWVVTAADV NSKFQVALPG KVVAGNNTSV GVSWSGLAPN
GRYVGGVHFT DASNVIQATT AVRVETGSAS IPTPQSERTQ LKLRD
//
