ID A0A178MWY1_9PROT Unreviewed; 408 AA.
AC A0A178MWY1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN ORFNames=A6A05_08050 {ECO:0000313|EMBL:OAN55698.1};
OS Magnetospirillum moscoviense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1437059 {ECO:0000313|EMBL:OAN55698.1, ECO:0000313|Proteomes:UP000078543};
RN [1] {ECO:0000313|EMBL:OAN55698.1, ECO:0000313|Proteomes:UP000078543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BB-1 {ECO:0000313|EMBL:OAN55698.1,
RC ECO:0000313|Proteomes:UP000078543};
RA Koziaeva V., Dziuba M.V., Ivanov T.M., Kuznetsov B., Grouzdev D.S.;
RT "Draft genome sequence of freshwater magnetotactic bacteria
RT Magnetospirillum marisnigri SP-1 and Magnetospirillum moscoviense BB-1.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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:OAN55698.1}.
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DR EMBL; LWQU01000095; OAN55698.1; -; Genomic_DNA.
DR RefSeq; WP_068497836.1; NZ_LWQU01000095.1.
DR AlphaFoldDB; A0A178MWY1; -.
DR STRING; 1437059.A6A05_08050; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000078543; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 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; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR NCBIfam; TIGR00225; prc; 1.
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 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Reference proteome {ECO:0000313|Proteomes:UP000078543};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..408
FT /note="PDZ domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008092318"
FT DOMAIN 126..182
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 408 AA; 43202 MW; 034E588665982924 CRC64;
MNRLFLAAFS VLVLISGASL ADRADRALLT QAFTQAGLET PKAKAKAELL DEMIAKIVEV
YVEPKESHQI SEAAAKAVRE LKPPQSPDDA FKAATGAMSE VLDPHTAYLT PADMDDMRTS
FSGQFGGVGM ELTMKEDQVV VVAPIDDTPA ARAGIKVDDR ILKVDGTPTA GQSLMQVVSK
IRGKVGTPVT LTLSTTNGVT RDVVLKREII QLQAVKGRLD GSDVAYVRVT QFAGGTAANL
RSTLLDLEKA AGGRLKGIVL DLRRNPGGLL DQAIAVADLF LGDVPIVSTT GRRSQDRQVY
SGRIGEIMAG LPIVVLIDGG SASASEIVAG ALKDHRRAVL VGQKSFGKGS VQTILDLSEG
GMRVTTSRYL RPSTQPVDKV GITPDIVTEP VEGSDPQLDR ALKVVRGN
//
