ID V2XZJ9_9FIRM Unreviewed; 623 AA.
AC V2XZJ9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=PDZ domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=N510_002799 {ECO:0000313|EMBL:USF27842.1}, N510_00403
GN {ECO:0000313|EMBL:ESL15134.1};
OS Firmicutes bacterium ASF500.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1378168 {ECO:0000313|EMBL:ESL15134.1};
RN [1] {ECO:0000313|EMBL:ESL15134.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF500 {ECO:0000313|EMBL:ESL15134.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF27842.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF500 {ECO:0000313|EMBL:USF27842.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AYJP01000004; ESL15134.1; -; Genomic_DNA.
DR EMBL; CP097573; USF27842.1; -; Genomic_DNA.
DR AlphaFoldDB; V2XZJ9; -.
DR STRING; 1378168.N510_00403; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_030019_0_0_9; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000017395; Chromosome.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd06567; Peptidase_S41; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001119; SLH_dom.
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; PF17820; PDZ_6; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF00395; SLH; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS51272; SLH; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Reference proteome {ECO:0000313|Proteomes:UP000017395};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..623
FT /note="PDZ domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004712673"
FT DOMAIN 75..155
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 436..495
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 496..559
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
SQ SEQUENCE 623 AA; 66863 MW; 05280B980FAD25CA CRC64;
MKKAISTLLA LVLGLSLAVL PASALELEEA KELLAVYYVD GVPPEVLELD SLDAILEALG
DPYTYYMTPE QYDWFNQSVN GRVVVGIGAT VENAFAGGYR VMSVLPQSPA LEAGLQPGDL
LVAVNGLELT AETDPRTYIV GQEGTSVTIT VVREGVRLDF TLTRRAVTIP IVTYEAQGGA
GYIECISFGE TTADTFEEAI KALEDHAEVW IVDLRANPGG DSKATAATAG HFVGSGIMLY
FRDGAGDYNY TFTLPGYPDL TDKPVIVLTS EHSASGSELF AGDIRAYEAG IALGQRTFGK
GTAQIVLEER NCEYMEGGEA MKITAYRFFA PDGATNHITG VLPTLLISLE NTQRAALLLS
CGLPDSPENH LKLELAGQTF CVSLSEALTE ENRPAFTELL EALPPSARLW HSTGQSWEDC
APITPAALAG TLGLSFTPRT LPDAADSEFA REIDTLTTYG IVSGFEDGLF HPGGTLTRAQ
FCAMTASALA LPDSARKDRF ADVSPDSWYA GAVNAMADMG FVSGYGDGTF RPEATVSFQE
MAVILNKAAA WASMDGYDLD REDLTVEEWG AYYDYADWAQ TAVRNLDKLG ALAGELDPAD
PGTREVAAAM ICRLMESIHL IWD
//