ID A0A1U7NEC0_9FIRM Unreviewed; 486 AA.
AC A0A1U7NEC0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN ORFNames=BO222_09645 {ECO:0000313|EMBL:OLU37836.1};
OS Ileibacterium valens.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Ileibacterium.
OX NCBI_TaxID=1862668 {ECO:0000313|EMBL:OLU37836.1, ECO:0000313|Proteomes:UP000186341};
RN [1] {ECO:0000313|EMBL:OLU37836.1, ECO:0000313|Proteomes:UP000186341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NYU-BL-A3 {ECO:0000313|EMBL:OLU37836.1,
RC ECO:0000313|Proteomes:UP000186341};
RA Cox L.M., Sohn J., Tyrrell K.L., Citron D.M., Lawson P.A., Patel N.B.,
RA Iizumi T., Perez-Perez G.I., Goldstein E.J., Blaser M.J.;
RT "Description of two novel members of the family Erysipelotrichaceae:
RT Ileibacterium lipovorans gen. nov., sp. nov. and Dubosiella newyorkensis,
RT gen. nov., sp. nov.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179}.
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:OLU37836.1}.
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DR EMBL; MPJW01000189; OLU37836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7NEC0; -.
DR Proteomes; UP000186341; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00989; PDZ_metalloprotease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR InterPro; IPR005151; Tail-specific_protease.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Reference proteome {ECO:0000313|Proteomes:UP000186341};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..172
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 486 AA; 53025 MW; 4EE86C73E9C6C4A6 CRC64;
MGPKTGNGQD DQKKRKIIAY SVLGIILAGM IAAGSLIYFK GSGSSSSKGL SKLEQIYELM
KSQWYYADTL EDPENDLIEG AILGMTMQPE DLHTNYFSLD EAEQFSKSLA GSNAGVGIVF
YEDADGNAVV RDVFVNSTAD QAGLKAGDII VKMNDQTISD LSSDELVSYI QKNEGRPIET
EFIRNGETNT VKLIPGVYDS TVSMQLHDNY GLVTLSSFSE MSGKEFADSL GRIREAGLNN
LVIDLRDNTG GYLSAAMDIA GSLLPSESPI FVEKDKEGNE KTFKSSKNYT QVPFEHIYVL
QNGSTASASE VLIGALKETL GEDVVTTIGQ KTYGKGTEQV SIPFEDGTSL KYTIAEWTTP
NGVSINKTGF TPDIETPVHA VASTRYQDMA DDESIEPDTV APNAAAVQVY LSYLSYPANR
DDTYFSVESS EALKSFQTDH GLDANGVVDK NTFDRLREEV ILKYNQNLTS EDETMQKAIE
LIDSND
//
