Y1991_PASMU
ID Y1991_PASMU Reviewed; 442 AA.
AC Q9CJL2;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Putative zinc metalloprotease PM1991;
DE EC=3.4.24.-;
GN OrderedLocusNames=PM1991;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; AE004439; AAK04075.1; -; Genomic_DNA.
DR RefSeq; WP_010907438.1; NC_002663.1.
DR AlphaFoldDB; Q9CJL2; -.
DR SMR; Q9CJL2; -.
DR STRING; 747.DR93_2108; -.
DR EnsemblBacteria; AAK04075; AAK04075; PM1991.
DR KEGG; pmu:PM1991; -.
DR PATRIC; fig|272843.6.peg.2014; -.
DR HOGENOM; CLU_025778_0_2_6; -.
DR OMA; QYMVGFG; -.
DR Proteomes; UP000000809; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837; PTHR42837; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 2.
DR TIGRFAMs; TIGR00054; TIGR00054; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..442
FT /note="Putative zinc metalloprotease PM1991"
FT /id="PRO_0000088452"
FT TRANSMEM 97..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 198..286
FT /note="PDZ"
FT ACT_SITE 22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 442 AA; 48609 MW; 915E65C99AD4E150 CRC64;
MSFLWSFASF IIVISVLVAV HEYGHFWAAR KCGIQVHRFS IGFGKVLWSR TDKQGTEFVI
SAIPLGGYVK MLDGRNEVVP PELSSRAFDQ KSVLQRAFVI AAGPIANFLF AILAYFTIYT
VGIPTVKPVI ADISSNSIAA QAQIEPNTQI MAVDGTKVSD WETINMLLAT KMGNDEIHLT
LSPFGSSIEQ HKVLNTKDWR FDPEKESAMS SLGLQPVRTK VDMILSKVEV NSPADKAGLK
AGDRIYAGEQ LISWQQFVQF VQEGKPFNVK VERDGQFSFV VLTPELNKKG RWYVGIAPTA
APISDIYRTE LKYGILEALQ KGVEKTIQLS WLTIKVIGKL FTGDLALKNL GGPISIAKGA
GISSEIGLIY YLGFMALISV NLGIMNLFPL PVLDGGHLVF LAAEAVRGKP LSERIQNLSY
RIGAAILMAL MGFALFNDFL RL