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Database: UniProt
Entry: A0A0S9PZ17_9ACTN
LinkDB: A0A0S9PZ17_9ACTN
Original site: A0A0S9PZ17_9ACTN 
ID   A0A0S9PZ17_9ACTN        Unreviewed;       977 AA.
AC   A0A0S9PZ17;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Peptidase M23 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASF47_17825 {ECO:0000313|EMBL:KQP62872.1};
OS   Nocardioides sp. Leaf285.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736322 {ECO:0000313|EMBL:KQP62872.1, ECO:0000313|Proteomes:UP000051495};
RN   [1] {ECO:0000313|EMBL:KQP62872.1, ECO:0000313|Proteomes:UP000051495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf285 {ECO:0000313|EMBL:KQP62872.1,
RC   ECO:0000313|Proteomes:UP000051495};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP62872.1, ECO:0000313|Proteomes:UP000051495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf285 {ECO:0000313|EMBL:KQP62872.1,
RC   ECO:0000313|Proteomes:UP000051495};
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   -!- 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:KQP62872.1}.
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DR   EMBL; LMNH01000005; KQP62872.1; -; Genomic_DNA.
DR   RefSeq; WP_056865386.1; NZ_LMNH01000005.1.
DR   AlphaFoldDB; A0A0S9PZ17; -.
DR   Proteomes; UP000051495; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd12797; M23_peptidase; 1.
DR   CDD; cd14814; Peptidase_M15; 1.
DR   CDD; cd13399; Slt35-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.30.1380.10; -; 1.
DR   Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR003709; Pept_M15B.
DR   InterPro; IPR016047; Peptidase_M23.
DR   InterPro; IPR031304; SLT_2.
DR   PANTHER; PTHR21666:SF270; OUTER MEMBRANE ANTIGENIC LIPOPROTEIN B; 1.
DR   PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   Pfam; PF13406; SLT_2; 1.
DR   Pfam; PF02557; VanY; 1.
DR   SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR   SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051495};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        216..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          540..590
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF13406"
FT   DOMAIN          697..789
FT                   /note="Peptidase M23"
FT                   /evidence="ECO:0000259|Pfam:PF01551"
FT   DOMAIN          860..974
FT                   /note="Peptidase M15B"
FT                   /evidence="ECO:0000259|Pfam:PF02557"
FT   REGION          1..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          624..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        657..675
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   977 AA;  98739 MW;  DCEAE98F6CB6395E CRC64;
     MPNADPASGE PSPARPNQGA PANQPRTPFS GRFEAPAETE TGGSSSKGFA HAFTTDKPRN
     PGGRRDASQP GRFANAFDKA LATGAAAASA GSGQGSAAGS AAGSDAPGTG SAGKPAFGAA
     SAAARARAAH AQEATPQGAR QQTKDASPFS GAFRLGGARG SGEDGKATVK DDVARTAEAA
     KQGASIGTKV GGPAGTAVGA AIGGVVGMAG SKRGRVLLAL GLLTGPLGVA AAITLVLVIV
     VAAIGGGFAG NQQSSAAVGV AAATEDGLTQ DQTAMAMNIA AVYNVPWEIL AAVPFHLDVD
     PTGPAQSFTT AARSKAIEGD EPVGAMGLAF DPTQDYVDST GTTPIDFEGM TNPVTSMTWV
     ARALSNEMTG RDASDVTLDA GTVSTADRED IAAYDIELGT SDADKEEAED AKEHFTDALS
     SLPFAEAETL APVVYDIALT WHLGGRDECD TGASAASAPS SVAGIPQVAL DAYVSAAEKT
     GVAWYYLAGI GFVETQHGTY AGSAPDTEGN VVPKIIGIRL DGSNNTAVIR DTDNGALDGD
     TSYDRAVGPM QFIPSTWATM SADGNLDGES DPHNIWDTAL AAAQYLNASG AAKDISGAIR
     AYNHSDAYVA AVLEKAEEYK AAPAAPTSGA SAQPASANAP APTADAAAGG QQGAGDDSGD
     DSDSANGGWT QPLQPGTYTL TARFGEKSSY WTSFAVGHSG LDYAAPAGTQ VFAVNAGTVT
     RLGDGGSYGS NYMEITHGTV DGKQIVSRYA HMQTALVSQG DTVDSGQLIG EVGSEGNSTG
     PHLHLEITVG PPLANGDPNF VDPETFLANA GVPQATAGED CVPTSGDQNF ETGPDGAWGG
     FSNGKIPASA LQQLSFSPAL LRPDAAAALE ALNTEYKAEF GCDIGPVGGY RSYEEQVALY
     AQKPGLAATP GTSNHGWGLA VDLSGNCNGN GGINIFGTPA NDWMQANAGE YGWLFPSWAV
     RGGGREEPWH WQFAVVE
//
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