ID A0A0Q5CM96_9MICO Unreviewed; 1117 AA.
AC A0A0Q5CM96;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASF54_10060 {ECO:0000313|EMBL:KQQ28934.1};
OS Frondihabitans sp. Leaf304.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frondihabitans.
OX NCBI_TaxID=1736329 {ECO:0000313|EMBL:KQQ28934.1, ECO:0000313|Proteomes:UP000051456};
RN [1] {ECO:0000313|EMBL:KQQ28934.1, ECO:0000313|Proteomes:UP000051456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ28934.1,
RC ECO:0000313|Proteomes:UP000051456};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ28934.1, ECO:0000313|Proteomes:UP000051456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ28934.1,
RC ECO:0000313|Proteomes:UP000051456};
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:KQQ28934.1}.
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DR EMBL; LMNV01000002; KQQ28934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5CM96; -.
DR STRING; 1736329.ASF54_10060; -.
DR Proteomes; UP000051456; 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; cd07474; Peptidases_S8_subtilisin_Vpr-like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034213; S8_Vpr-like.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 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; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
DR PROSITE; PS51318; TAT; 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:UP000051456};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1117
FT /note="Peptidase S8/S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006245886"
FT DOMAIN 193..668
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 464..545
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 279
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 630
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1117 AA; 113409 MW; 8CF117E285655D09 CRC64;
MRPSRRSVGT LCVVAAATIA LVSTPLTVAS AAPANPLGSA SKTADLLKLS SPLREAKGSV
AAFIRVSGTG ALSVDASAKG GKLTGRPQST AAKNRVSAIR QNAAAVTKAL AAQGPKVTTL
YTTEYTVPGV AVIADAGSLA TIAARSDVVS ITPIAPKSIP TPVATKGEAS PLNSTSDVYT
RAVQAWQQTG HTGTGVNIAV IDTGLDYTHA DFGGPGTTAA YDEALSSTGA PDPALFDSAK
FLGGTDFAGP TYDADPSSQA YDPVPNPDAN PIDGRGGGHG SHVAGTAAGF GLDSDKKTFT
GDYTKLTEDE VKTMSIGPGT APDAGLYSLK VFGDGGGSTD LTGAALDWVG QALTEGKDIN
VINLSLGSDY SNPDDPDNAK IDSLVARGVL PVIASGNAGD FTDIGGSPGD AENALTVAAA
TTGAAVFDGV DVTAPSSVAG TIRAQYSISY TKPLALTDGV VTLPSAANAA GCDPYTAADA
AKVKGKVVLL KWTDTALECG SVKRFDNATA AGAIGVLLGG SVNVFDAGIS GNAVIPGAEI
TKDAYAKLLP AVTAAEAGGT PVTVSFKDSL RLFDQAIDST LTDTLATFSS RGVHGSYSNI
IKPDVAAPGV NVVSVRSGTG TDREAESGTS MATPDTAGIA ALTFEAHDGW SALQVKQAVM
NTATHDLKNA AGTLYSTLSQ GTGRIDALQA VTNQVTVTST QNAGLVSASF GVVPVSAAKT
ATRTLTLHNS GNASQTFTTS YSSRITQPGV SFTLSAPKVV VPARGDATVT LTMKIDPSKL
RKVIDPTQDA TTNVSGVDFV REFVAAASGY VKFDSADRTK SGLRLSVFAA PKPVSANAAT
SPVFAKSTST QATLKISGTT LNQGTGSQAY LGLAAPFVLG ANSAKLTFPT GSPKQSLAGA
DILAVGASSN APNLTDKNKG IVSFGIKTAG PIANPGLDGA PEVFIDTNRD GTDDFVSYVT
KSASVDATFV ATDNLSTNET VDLQPYNANY LDKDVNTFDS SVAVLPVSLA ALGYTTKSKS
TAFNYHVATF SNYAPGLAET DSTVVDSTHS ASFDALKPSL WFSQKKADDL GGVLLRDQSP
GIAVHRTKAS TKQILLLHLH NAVAKQAQTV TVTTKKK
//