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Database: UniProt
Entry: A0A0Q8XJS0_9SPHN
LinkDB: A0A0Q8XJS0_9SPHN
Original site: A0A0Q8XJS0_9SPHN 
ID   A0A0Q8XJS0_9SPHN        Unreviewed;       436 AA.
AC   A0A0Q8XJS0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Peptidase M20 {ECO:0000313|EMBL:KRC80073.1};
GN   ORFNames=ASE13_13670 {ECO:0000313|EMBL:KRC80073.1};
OS   Sphingomonas sp. Root241.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736501 {ECO:0000313|EMBL:KRC80073.1, ECO:0000313|Proteomes:UP000051629};
RN   [1] {ECO:0000313|EMBL:KRC80073.1, ECO:0000313|Proteomes:UP000051629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root241 {ECO:0000313|EMBL:KRC80073.1,
RC   ECO:0000313|Proteomes:UP000051629};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC80073.1, ECO:0000313|Proteomes:UP000051629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root241 {ECO:0000313|EMBL:KRC80073.1,
RC   ECO:0000313|Proteomes:UP000051629};
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:KRC80073.1}.
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DR   EMBL; LMIV01000002; KRC80073.1; -; Genomic_DNA.
DR   RefSeq; WP_056616790.1; NZ_LMIV01000002.1.
DR   AlphaFoldDB; A0A0Q8XJS0; -.
DR   STRING; 1736501.ASE13_13670; -.
DR   OrthoDB; 9777385at2; -.
DR   Proteomes; UP000051629; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR   PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..436
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006362323"
FT   DOMAIN          210..309
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   436 AA;  46415 MW;  0B3431B9E19B1E18 CRC64;
     MRTLLTAALA MTLATPANAA DPVHQATQAA LPQLMDFYRD FHANPELSLH EIRTAAKLAA
     EARKAGYEVT EKVGGTGVVA VLKNGAGPIL LIRADMDGLP VTEDTGLPFA SKVRTTNDEG
     IETGVMHACG HDTHMASWIG TLRNLAAMKS QWKGTLVMIA QPAEERGMGA RMMLEDGLFT
     RFPKPQFALA FHDAAALPAG TIGVRSGYAL ANVDSVDIKV SGVGGHGAYP QTTRDPIILA
     ARIVTTLQTL VSREIDPQDA AVVTVGAIHG GSTHNIIGKE VTMLLTVRSY TPEVRKKLLD
     GIARIAKGEA IAAGIPEDRM PVVTIRNEGT PSTFNTEPLT GRLQALWTGR FGKDRVVETP
     AVMGGEDFGR FYLADKSIQS MIFWVGGVPK AKWDAAQAGK EPLPSLHSPF WAPEAEAVIG
     TATEAMTAAA LDILKR
//
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