ID G7M7L6_9CLOT Unreviewed; 452 AA.
AC G7M7L6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=CHAP domain containing protein {ECO:0000313|EMBL:EHJ02405.1};
GN ORFNames=CDLVIII_5942 {ECO:0000313|EMBL:EHJ02405.1};
OS Clostridium sp. DL-VIII.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=641107 {ECO:0000313|EMBL:EHJ02405.1, ECO:0000313|Proteomes:UP000005106};
RN [1] {ECO:0000313|EMBL:EHJ02405.1, ECO:0000313|Proteomes:UP000005106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DL-VIII {ECO:0000313|EMBL:EHJ02405.1,
RC ECO:0000313|Proteomes:UP000005106};
RX PubMed=23929491;
RA Taghavi S., Izquierdo J.A., van der Lelie D.;
RT "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL Genome Announc. 1:e00605-e00613(2013).
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DR EMBL; CM001240; EHJ02405.1; -; Genomic_DNA.
DR RefSeq; WP_009173041.1; NZ_CM001240.1.
DR AlphaFoldDB; G7M7L6; -.
DR STRING; 641107.CDLVIII_5942; -.
DR eggNOG; COG3942; Bacteria.
DR eggNOG; COG5263; Bacteria.
DR HOGENOM; CLU_653297_0_0_9; -.
DR Proteomes; UP000005106; Chromosome.
DR Gene3D; 2.10.270.20; -; 1.
DR Gene3D; 2.10.270.10; Cholin Binding; 1.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR InterPro; IPR007921; CHAP_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003646; SH3-like_bac-type.
DR Pfam; PF05257; CHAP; 1.
DR Pfam; PF19127; Choline_bind_3; 2.
DR Pfam; PF08239; SH3_3; 1.
DR SMART; SM00287; SH3b; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50911; CHAP; 1.
DR PROSITE; PS51170; CW; 4.
DR PROSITE; PS51781; SH3B; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000005106};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 48..67
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 68..87
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 88..107
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 108..127
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT DOMAIN 173..238
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 317..446
FT /note="Peptidase C51"
FT /evidence="ECO:0000259|PROSITE:PS50911"
FT REGION 148..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 50196 MW; F914752EA1650A7C CRC64;
MKRELLRKII AVGMTTLIVS SLNYMPASAK WISNSNNSWN WTEDGIKATG WKNIDNKWYY
FDENGIMLTG WIKYSQNWYS LSNDGAMNTG WKNISGKWYH FDADGKMSTG WINDNGNRYF
MESSGEMVTG SLNIDGIVYN FSDNGQLIKD ENSDKENQSA PPVAQDSTSG AKPRIAYVTT
NSDSLNVRAE ATTSSDIIGK LAKGMQVSII DDAKGGFYPL MLNGRKGWVS SDWISFKEND
NSTTSNSTSP NGDSSGSSNV NPSDASNGND NKSNDDNKSD DNNNKSDGNN NDKNVKEVSL
GGIRTTEPSL NSKYYYSDDN IFYKVKLSPP FYSGGSQIKG NCTWYAWGRA WEITGTKPTD
AGLIGNAYEW WNANKNSGKY QYGSEPRVGA IAVWKSGLPN SGGSGHVAVV EKIDNGKVYI
SESTWNGVTF RYRDLYETDY LYGYIYLDKP NY
//