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Database: UniProt
Entry: A0A2R8AFM8_9RHOB
LinkDB: A0A2R8AFM8_9RHOB
Original site: A0A2R8AFM8_9RHOB 
ID   A0A2R8AFM8_9RHOB        Unreviewed;       513 AA.
AC   A0A2R8AFM8;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Peptidoglycan binding-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=POI8812_03394 {ECO:0000313|EMBL:SPF31044.1};
OS   Pontivivens insulae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pontivivens.
OX   NCBI_TaxID=1639689 {ECO:0000313|EMBL:SPF31044.1, ECO:0000313|Proteomes:UP000244932};
RN   [1] {ECO:0000313|EMBL:SPF31044.1, ECO:0000313|Proteomes:UP000244932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CeCT 8812 {ECO:0000313|EMBL:SPF31044.1,
RC   ECO:0000313|Proteomes:UP000244932};
RA   Keele B.F.;
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; OMKW01000004; SPF31044.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R8AFM8; -.
DR   OrthoDB; 8092964at2; -.
DR   Proteomes; UP000244932; Unassembled WGS sequence.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   InterPro; IPR011600; Pept_C14_caspase.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR22576:SF37; MALT1 PARACASPASE HOMOLOG; 1.
DR   PANTHER; PTHR22576; MUCOSA ASSOCIATED LYMPHOID TISSUE LYMPHOMA TRANSLOCATION PROTEIN 1/PARACASPASE; 1.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   Pfam; PF01471; PG_binding_1; 2.
DR   SUPFAM; SSF52129; Caspase-like; 1.
DR   SUPFAM; SSF47090; PGBD-like; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000244932};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..513
FT                   /note="Peptidoglycan binding-like domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015320966"
FT   DOMAIN          24..117
FT                   /note="Peptidase C14 caspase"
FT                   /evidence="ECO:0000259|Pfam:PF00656"
FT   DOMAIN          258..299
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   DOMAIN          452..506
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   REGION          218..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   513 AA;  55639 MW;  FCB873664E20EDAD CRC64;
     MFRIFRLALL ASTVSAAPLM ADPLALVITN SDYANGPQAT VPDHADLVRA YEEAGFTVEG
     GQDLTRAEMF TLLTSFQRDV ADAERLVIHL SGHTATAGGE TWFLPVDARD DSVVRLAFTM
     PTVDLFLDMA AEQEGRSVVF LGTATDAGLE GDGFEPGLGR VYVPTGALMV SGPAQAVADI
     ATDRALSEGA SFRSFVSDLP DDISRLGFAS PDATLVPLRE DLPDDLGEAP AEPQSEPEPD
     EQQVDPAEAT EQALELDRDD RVAIQENLVV LGYNTRGIDG IFGPGTRGAI SAWQGEQDFE
     GTSFLTAGQL RLLGLQADNR RAEIAAEQER LRQQREAEDR AFWQSSGSDG SEEGLRVYLR
     NYPNGLFAAE AQTQLDAIEA EQRALASAEV QAAWQSAMET NTIEGYEQFL AQYPDSEFAT
     TARARIDQIN EQENRVDANL QAQEDALGLN TANRLLVQVR LASLGYAIPS VNGRFDAATR
     EAIAQFQREY GQEPTGYLNQ TTVRQLITLA PAE
//
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