ID   Q8Y649_LISMO            Unreviewed;       496 AA.
AC   Q8Y649;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 129.
DE   SubName: Full=Lmo1851 protein {ECO:0000313|EMBL:CAC99929.1};
GN   OrderedLocusNames=lmo1851 {ECO:0000313|EMBL:CAC99929.1};
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963 {ECO:0000313|EMBL:CAC99929.1, ECO:0000313|Proteomes:UP000000817};
RN   [1] {ECO:0000313|EMBL:CAC99929.1, ECO:0000313|Proteomes:UP000000817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e {ECO:0000313|Proteomes:UP000000817};
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., Portillo F.G., Garrido P., Gautier L., Goebel W., Gomez-Lopez N.,
RA   Hain T., Hauf J., Jackson D., Jones L.M., Kaerst U., Kreft J., Kuhn M.,
RA   Kunst F., Kurapkat G., Madueno E., Maitournam A., Vicente J.M., Ng E.,
RA   Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.C.,
RA   Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA   Vazquez-Boland J.A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
CC   -!- SIMILARITY: Belongs to the peptidase S41A family.
CC       {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR   EMBL; AL591981; CAC99929.1; -; Genomic_DNA.
DR   PIR; AC1306; AC1306.
DR   RefSeq; NP_465376.1; NC_003210.1.
DR   RefSeq; WP_003733072.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y649; -.
DR   STRING; 169963.gene:17594536; -.
DR   MEROPS; S41.007; -.
DR   PaxDb; 169963-lmo1851; -.
DR   DNASU; 985844; -.
DR   EnsemblBacteria; CAC99929; CAC99929; CAC99929.
DR   GeneID; 985844; -.
DR   KEGG; lmo:lmo1851; -.
DR   PATRIC; fig|169963.11.peg.1896; -.
DR   eggNOG; COG0793; Bacteria.
DR   eggNOG; COG3409; Bacteria.
DR   HOGENOM; CLU_017295_3_0_9; -.
DR   OrthoDB; 9812068at2; -.
DR   PhylomeDB; Q8Y649; -.
DR   BioCyc; LMON169963:LMO1851-MONOMER; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 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; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
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   Pfam; PF01471; PG_binding_1; 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   SUPFAM; SSF47090; PGBD-like; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU004404};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU004404};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000817};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU004404}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          111..187
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  54137 MW;  A9B49F893C0214EB CRC64;
     MEESPQNEPN KVEKDEEQKS KPGNGYIKMK LFPFIMLLFA FVFVTALVTT IVMSLGDDKQ
     VKVSIPERKE FTKLYDVYDE ITSKYYKDTN STTMIDGAIS GMVNSLDDPY STFMSKKESS
     EFNDTISASF EGIGAEIQEK DGAIVIVSPI KNSPAEKAGL RPQDIITQVD GKSVKGDTAT
     EATQKIRGEK GTKVTLTIQR SNEDKPFDVT ITRDEIPIET VYKEMGSDKI AHVTISTFSE
     TTYDELEKAL KSLEKDGMKG LVLDLRGNPG GLLDQAVSIS SLFVPDGKIV VQEQDKDGDK
     SAIKADSSSH GDYKVKVPTT MLIDGGSASA SEILAAAAKE SGGIKLVGTK SFGKGTVQTA
     TTLSDDSTLK LTVAKWLTPN SEWIHEKGIT PDVVVNMPDY ATMTIPSSTK VYKNGDFGDD
     VKTIETLLKA LDYNVGKVDG LYDTDTEYAV QRFQTANKLD VTGIMTGVTT DKLVELTQKH
     LKETDPQLQK AKALVK
//