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Database: UniProt
Entry: A0A0Q8XHD1_9SPHN
LinkDB: A0A0Q8XHD1_9SPHN
Original site: A0A0Q8XHD1_9SPHN 
ID   A0A0Q8XHD1_9SPHN        Unreviewed;       429 AA.
AC   A0A0Q8XHD1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Peptidase M28 {ECO:0000313|EMBL:KRC81500.1};
GN   ORFNames=ASE13_03700 {ECO:0000313|EMBL:KRC81500.1};
OS   Sphingomonas sp. Root241.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736501 {ECO:0000313|EMBL:KRC81500.1, ECO:0000313|Proteomes:UP000051629};
RN   [1] {ECO:0000313|EMBL:KRC81500.1, ECO:0000313|Proteomes:UP000051629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root241 {ECO:0000313|EMBL:KRC81500.1,
RC   ECO:0000313|Proteomes:UP000051629};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC81500.1, ECO:0000313|Proteomes:UP000051629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root241 {ECO:0000313|EMBL:KRC81500.1,
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:KRC81500.1}.
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DR   EMBL; LMIV01000001; KRC81500.1; -; Genomic_DNA.
DR   RefSeq; WP_056611595.1; NZ_LMIV01000001.1.
DR   AlphaFoldDB; A0A0Q8XHD1; -.
DR   STRING; 1736501.ASE13_03700; -.
DR   OrthoDB; 9787436at2; -.
DR   Proteomes; UP000051629; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..429
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006362209"
FT   DOMAIN          100..201
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   429 AA;  45611 MW;  9635D2B78FACB947 CRC64;
     MRILAILPVL LLATPAAAQT QPSPTRLKAS VEKLVSFGTR HTLSSPDHPT RGVGAARRWF
     ATELSRIGEG CGGCIETANL ARTFTNDRAP NGVEVVDVLG FQPGRNAKRV VIVMGHIDSR
     VSDPMNATSD APGANDDASG VALVLEAARI LSKEKFDATI VYAALSGEEQ GLFGGQLLAE
     TAKERGWTVS AVLNNDIVGN TIGQDGSRVA DRVRLFSEGI RQVESLDEQI ARRADGGEDD
     GPSRALAKAA DGVAGKLPGG LDVVLVRRPD RFGRGGDHTP FLKLGYPAVR FTVGVENYDA
     QHQDLRTENG RIYGDTIDRM DFAYLAKVTA INVATIRRLA SAPAAPASVT IGGALASDTS
     VKWEPVPGAS RYRVHWRRAD AQEWQHHVDV AGAETVLKGV IVDDHFVGVS ALAADGSESL
     VTFGGRARR
//
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