PRTA_LISMO
ID PRTA_LISMO Reviewed; 510 AA.
AC P23224;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Zinc metalloproteinase;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=mpl; Synonyms=prtA; OrderedLocusNames=lmo0203;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EGD / Serovar 1/2a;
RX PubMed=1898903; DOI=10.1128/iai.59.1.65-72.1991;
RA Domann E., Leimeister-Waechter M., Goebel W., Chakraborty T.;
RT "Molecular cloning, sequencing, and identification of a metalloprotease
RT gene from Listeria monocytogenes that is species specific and physically
RT linked to the listeriolysin gene.";
RL Infect. Immun. 59:65-72(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=2509367; DOI=10.1128/iai.57.12.3695-3701.1989;
RA Mengaud J., Vicente M.-F., Cossart P.;
RT "Transcriptional mapping and nucleotide sequence of the Listeria
RT monocytogenes hlyA region reveal structural features that may be involved
RT in regulation.";
RL Infect. Immun. 57:3695-3701(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
CC -!- FUNCTION: Probably linked to the pathogenesis of listerial infection.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: The mpl and the listeriolysin genes being physically linked,
CC their expression may be regulated in a similar manner.
CC -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR EMBL; X54619; CAA38439.1; -; Genomic_DNA.
DR EMBL; AL591974; CAD00730.1; -; Genomic_DNA.
DR PIR; A43575; A60280.
DR PIR; AD1100; AD1100.
DR RefSeq; NP_463734.1; NC_003210.1.
DR RefSeq; WP_010989373.1; NZ_CP023861.1.
DR AlphaFoldDB; P23224; -.
DR SMR; P23224; -.
DR STRING; 169963.lmo0203; -.
DR MEROPS; M04.008; -.
DR PaxDb; P23224; -.
DR EnsemblBacteria; CAD00730; CAD00730; CAD00730.
DR GeneID; 987034; -.
DR KEGG; lmo:lmo0203; -.
DR PATRIC; fig|169963.11.peg.208; -.
DR eggNOG; COG3227; Bacteria.
DR HOGENOM; CLU_008590_5_2_9; -.
DR OMA; HMKDYES; -.
DR PhylomeDB; P23224; -.
DR BioCyc; LMON169963:LMO0203-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005576; C:extracellular region; 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; 1.10.390.10; -; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR025711; PepSY.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF03413; PepSY; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..200
FT /evidence="ECO:0000255"
FT /id="PRO_0000028632"
FT CHAIN 201..510
FT /note="Zinc metalloproteinase"
FT /id="PRO_0000028633"
FT ACT_SITE 350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 437
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CONFLICT 186
FT /note="V -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="L -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 57411 MW; FF978FBDCAA804C0 CRC64;
MKSKLICIIM VIAFQAHFTM TVKADSVGEE KLQNNTQAKK TPADLKALPD SCEAKDFYKN
FKILDMTKDK LGVTHYTLAL SSGGYLTDND EIKVHVTPDN KITFINGDLQ QGQLRITNQI
KITEKNAIEK AFEAIGQSEA HVKSYVGNPV KEKEIILNSR TKRLVYNIKL IFAEPEVASW
IVQVDVETGA ILKKQNMLSE VERADTHKDF QALGKGANRL LQRPLHVMKI NDLFYLVDRT
HKGLIRTFDL KHNTDTSFGK VVSNKTNMFT DPEFSSAVDA HFYASEVYEY YKNVHQLESL
DGKGGEIDSF VHYGLNCNNA FWDGQEILYG DGDKKNFKPF SCAKTIVGHE LTHAVIQYSA
GLEYEGQSGA LNESFADVFG YFIAPNHWLI GEDVCVRGSR DGRIRSIKDP DKYNQAAHMK
DYESLPLTEE GDWGGVHYNS GIPNKAAYNT ITKLGKEKTE QLYFRALKYY LTKKSQFTDA
KKALQQAAKD LYGEDASKKV AEAWEAVGVN
