ID A0A0Q8EAA3_9ACTN Unreviewed; 1003 AA.
AC A0A0Q8EAA3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Serine protease {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASD81_10865 {ECO:0000313|EMBL:KRA39050.1};
OS Nocardioides sp. Root614.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736571 {ECO:0000313|EMBL:KRA39050.1, ECO:0000313|Proteomes:UP000051699};
RN [1] {ECO:0000313|EMBL:KRA39050.1, ECO:0000313|Proteomes:UP000051699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root614 {ECO:0000313|EMBL:KRA39050.1,
RC ECO:0000313|Proteomes:UP000051699};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA39050.1, ECO:0000313|Proteomes:UP000051699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root614 {ECO:0000313|EMBL:KRA39050.1,
RC ECO:0000313|Proteomes:UP000051699};
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 -!- 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:KRA39050.1}.
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DR EMBL; LMGV01000001; KRA39050.1; -; Genomic_DNA.
DR RefSeq; WP_056710035.1; NZ_LMGV01000001.1.
DR AlphaFoldDB; A0A0Q8EAA3; -.
DR OrthoDB; 614750at2; -.
DR Proteomes; UP000051699; 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; 3.40.50.200; 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; 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; 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; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 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:UP000051699};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 100..159
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 187..663
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 458..527
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 206..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 286
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 610
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1003 AA; 102976 MW; 94364BE47EEBD8A6 CRC64;
MQDLRTGARA RRLPSLLVLA LAATLGLTVT LGAPALADPS DPGPGAADGE GQSAVKADLT
RYKAGRYVVM LAAPPASTAG PTRAGAGEQF DAKGAGVASY TKKLRASHEK LGTDLGFDVK
VHYTISANGF VADLTAKQAT ELATDRRVLT VQKDSIVYAD TWNTPDFLGL TGKRGVWNQV
GGQDKAGDGV VVGVIDSGIW PESKSFKGSK LTSKPQGKWG TKISGSITSM KKSDGNLFRG
ECETGEEFTL ANCNTKLISA RSFVEGYGES RTVEEDYLSA RDGNGHGSHT ASTSAGNPVK
DVATEGVTFG NISGVAPAAK IAVYKALWAT EDGRASGTTS DLVAAIEQAV TDGVDVLNYS
ISGPTDTVLE AAEIAFEGAA EAGVFVAASA GNEGPGASTV AHNSPWVTTV AASTHTSFEN
TVVLGDGQKL VGASISRTAL PDTKLVDAAD VGNGSAPDTA LCPPNSLDPA KVAGTIVVCQ
RGVYDRVVKS EEVKRAGGVG VVLANITDGS LDADFHAVPT IHVSHVDSPK VYDYLESAGA
GATARFELGN LTGTVTPVPQ IAGFSSRGPA ASDDSDLLKP DISAPGVSVL AAVAPPSNHG
RDYDLYSGTS MSAPHIAGLA ALIQGKHPKW TPMQIKSAMM TTATDLKTAT GAKSTDLFAQ
GAGHVNAKAF LDPGLFVLSD WEQWYGYITG LGLDTGVPAI EPNAVNLPSL AEGHVMTEVS
LNRTFTAARK GTWKVKVEVP GFKSTASRSS VVAKKAGQET TVGFTFQRTT APLSQWAFGH
VTLTGPTTVR LPVALRPVSV KAPTSIDGTG TDGSTNVPIT GGFNGDLQVS TAGLVKGQVA
EGALAVGDYA LECVTIGEGN DLAQFDLVAP DQTSDLDMFV YAASSCDPAT IFAVAGEVAT
PSPGETFSLE GAPAGTYLVE VDAFAAGDQG APVPYSLRVY DLGGTPSVGN LAVDPNPVPV
TTGGDTSFDV SWSGLDAEAH YFGLLGYDGA PNSTFVYVDT ATP
//
