ID A0A0H2UZ70_SHIFL Unreviewed; 680 AA.
AC A0A0H2UZ70;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Carboxy-terminal protease for penicillin-binding protein 3 {ECO:0000313|EMBL:AAN42996.2};
GN Name=prc {ECO:0000313|EMBL:AAN42996.2};
GN OrderedLocusNames=SF1395 {ECO:0000313|EMBL:AAN42996.2};
OS Shigella flexneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623 {ECO:0000313|EMBL:AAN42996.2, ECO:0000313|Proteomes:UP000001006};
RN [1] {ECO:0000313|EMBL:AAN42996.2, ECO:0000313|Proteomes:UP000001006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a {ECO:0000313|Proteomes:UP000001006};
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR EMBL; AE005674; AAN42996.2; -; Genomic_DNA.
DR RefSeq; NP_707289.4; NC_004337.2.
DR AlphaFoldDB; A0A0H2UZ70; -.
DR PaxDb; 198214-SF1395; -.
DR GeneID; 1024381; -.
DR KEGG; sfl:SF1395; -.
DR PATRIC; fig|198214.7.peg.1645; -.
DR HOGENOM; CLU_016199_1_0_6; -.
DR Proteomes; UP000001006; Chromosome.
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; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR InterPro; IPR020992; Tail_Prtase_C.
DR InterPro; IPR040573; TSP_N.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR PANTHER; PTHR32060:SF32; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF11818; DUF3340; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF17804; TSP_NTD; 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, ECO:0000313|EMBL:AAN42996.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001006};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..680
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002599817"
FT DOMAIN 236..306
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 680 AA; 76438 MW; 4EDF82E2646833B5 CRC64;
MFFRLTALAG LLAIAGQTFA VEDITRADQI PVLKEETQHA TVSERVTSRF TRSHYRQFDL
DQAFSAKIFD RYLNLLDYSH NVLLASDVEQ FAKKKTELGD ELRSGKLDVF YDLYNLAQKR
RFERYQYALS VLEKPMDFTG NDTYNLDRSK APWPKNEAEL NAQWDSKVKF DELSLKLTGK
TDKEIRETLT RRYKFAIRRL AQTNSEDVFS LAMTAFAREI DPHTNYLSRR NTEQFNTEMS
LSLEGIGAVL QMDDDYTVIN SMVAGGPAAK SKAISVGAKI VGVGQTGKPM VDVIGWRLDD
VVALIKGPKG SKVRLEILPA GKGTKTRTVT LTRERIRLED RAVKMSVKTV GKEKVGVLDI
PGFYVGLTDD VKVQLQKLEK QNVSSVIIDL RSNGGGALTE AVSLSGLFIP AGPIVQVRDN
NGKVREDSDT DGQVFYKGPL VVLVDRFSAS ASEIFAAAMQ DYGRALVVGE PTFGKGTVQQ
YRSLNRIYDQ MLRPEWPALG SVQYTIQKFY RVNGGSTQRK GVTPDIIMPT GNEETETGEK
FEDNALPWDS IDAATYVKSG DLTAFEPELL KEHNARIAKD PEFQNIMKDI ARFNAMKDKR
NIVSLNYAVR EKENNEDDAT RLARLNERFK REGKPELKKL DDLSKDYQEP DPYLDETVNI
ALDLAKLEKA RPAEQPAPVK
//