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Database: UniProt
Entry: A0A160KU67_9MICO
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Original site: A0A160KU67_9MICO 
ID   A0A160KU67_9MICO        Unreviewed;       987 AA.
AC   A0A160KU67;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Gram-positive cocci surface proteins LPxTG domain-containing protein {ECO:0000259|PROSITE:PS50847};
GN   ORFNames=A6122_2289 {ECO:0000313|EMBL:AND17410.1};
OS   Rathayibacter tritici.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=33888 {ECO:0000313|EMBL:AND17410.1, ECO:0000313|Proteomes:UP000077071};
RN   [1] {ECO:0000313|EMBL:AND17410.1, ECO:0000313|Proteomes:UP000077071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 1953 {ECO:0000313|EMBL:AND17410.1,
RC   ECO:0000313|Proteomes:UP000077071};
RA   Park J., Lee H.-H., Lee S.-W., Seo Y.-S.;
RT   "Complete genome sequence of Rathayibacter tritici NCPPB 1953.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   EMBL; CP015515; AND17410.1; -; Genomic_DNA.
DR   RefSeq; WP_068255211.1; NZ_PSWT01000001.1.
DR   AlphaFoldDB; A0A160KU67; -.
DR   STRING; 33888.A6122_2289; -.
DR   KEGG; rtn:A6122_2289; -.
DR   PATRIC; fig|33888.3.peg.2550; -.
DR   OrthoDB; 9758209at2; -.
DR   Proteomes; UP000077071; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR000834; Peptidase_M14.
DR   NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR   PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077071};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..987
FT                   /note="Gram-positive cocci surface proteins LPxTG domain-
FT                   containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007817028"
FT   TRANSMEM        959..977
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          949..987
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|PROSITE:PS50847"
FT   REGION          869..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..946
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   987 AA;  102252 MW;  61A787CDF3816F2F CRC64;
     MRSRTAFASG CAALALATGG LLVAPPATAT TAAPADYTRV DLVRPPSAPI TVPTSYPQQT
     PLTEVPVDPT DASLLRGVTP YDAIAPQLNA LAARSDRVST QVVGKSGLGR DIYLVTVTAA
     ETEAETAQQT QWRDRLKYEP AAAAADAELM ADYKVPVWFN GNIHGNEWEG SDAILEYIEG
     VATAEDPATE ALLEGNRLYF TVTNNPDGRA LGQRAVAAGY DPNRDMITGA TSEAAVIRDL
     SSVLQPTYFI DIHGYTGILQ VEPCGPPHGE NYEYDLFLPH AYATALEIER RVVEADVPGN
     TYLAEDGSAT AENTGTILIP YRDIRAGWDD WPPIFAPQYV AFQGAITNTV ELPLGRTANE
     TPEEVAQGQA NADIDVEVAG IVMDASVDYI EANRDALLSN QVAIFERGAT GAPAVEIPAD
     VSAADLPAGT PTEWTEIWDE TDVYTTEYPR AYVIPVDGTQ RSVSDAETLV AQLLAHGVEV
     SRTTAATSVG GVSYPAGTYL VDMHQSVRGL ANVLLADGSD ISSRVPEMYD VSAWSLSLLW
     GADVHAIGST SDPLPVVGLE PVTAIAPTGS VPAGADYLAF EPRGVLEYQA LNALLADGVA
     VEQFEDGTVA LRADAAGLTA AEAAAAVFGV DFTATTADRV RAEDGKALDA LRVAYSGTNE
     DRDALAKLGF ADAVAVDPDA LSTGTATLEG ADVLYVGRAL SFTPEQAAGR AVVEEFLAGG
     GDVVGRGGAG AAFVADFGLA TLTAQTGTRG SNGIVSVETP AGGVLGDYPQ DTAFVSPALW
     FAGFDDSVAV EQSYSAEGTF VAGHWVDSEG QSRSDAAGQA SAVSFSTESG TEGFLFGTSP
     VFRNHPVGAF SDIARALLAV APEGAAVELP GAAEPTPTPT PEPTLTHSPE PTGSPEPTAT
     PEPSMSPEPS MSPEPTATPE PTVGPEPTTA PDPTATAAPI PAPTGPGGLP STGVETGSWL
     LLSGGALAVG IGSLLIARRR RREDQEA
//
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