P60_LISMO
ID P60_LISMO Reviewed; 484 AA.
AC P21171; Q03493;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable endopeptidase p60;
DE EC=3.4.-.-;
DE AltName: Full=Invasion-associated protein p60;
DE Flags: Precursor;
GN Name=iap; OrderedLocusNames=lmo0582;
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], AND PROTEIN SEQUENCE OF 28-49.
RC STRAIN=EGD / Serovar 1/2a;
RX PubMed=2111287; DOI=10.1128/iai.58.6.1943-1950.1990;
RA Koehler S., Leimeister-Waechter M., Chakraborty T., Lottspeich F.,
RA Goebel W.;
RT "The gene coding for protein p60 of Listeria monocytogenes and its use as a
RT specific probe for Listeria monocytogenes.";
RL Infect. Immun. 58:1943-1950(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISCUSSION OF SEQUENCE.
RC STRAIN=EGD / Mackaness / Serovar 1/2a;
RX PubMed=1459966; DOI=10.1128/jb.174.24.8166-8171.1992;
RA Bubert A., Kuhn M., Goebel W., Koehler S.;
RT "Structural and functional properties of the p60 proteins from different
RT Listeria species.";
RL J. Bacteriol. 174:8166-8171(1992).
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=16247833; DOI=10.1002/pmic.200402075;
RA Pucciarelli M.G., Calvo E., Sabet C., Bierne H., Cossart P.,
RA Garcia-del Portillo F.;
RT "Identification of substrates of the Listeria monocytogenes sortases A and
RT B by a non-gel proteomic analysis.";
RL Proteomics 5:4808-4817(2005).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=22837151; DOI=10.2436/20.1501.01.157;
RA Mariscotti J.F., Quereda J.J., Pucciarelli M.G.;
RT "Contribution of sortase A to the regulation of Listeria monocytogenes
RT LPXTG surface proteins.";
RL Int. Microbiol. 15:43-51(2012).
CC -!- FUNCTION: This major extracellular protein may be involved in the
CC invasion of non-professional phagocytic cells by Listeria.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:16247833}.
CC Secreted {ECO:0000269|PubMed:22837151}.
CC -!- INDUCTION: Present in both exponential and stationary phase (at protein
CC level). {ECO:0000269|PubMed:16247833}.
CC -!- DOMAIN: LysM domains are thought to be involved in peptidoglycan
CC binding.
CC -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01284, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC98661.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X52268; CAA36509.1; -; Genomic_DNA.
DR EMBL; M80351; AAA25280.1; -; Genomic_DNA.
DR EMBL; AL591975; CAC98661.1; ALT_INIT; Genomic_DNA.
DR PIR; A41487; A41487.
DR PIR; AG1147; AG1147.
DR RefSeq; NP_464110.1; NC_003210.1.
DR AlphaFoldDB; P21171; -.
DR STRING; 169963.lmo0582; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR PaxDb; P21171; -.
DR EnsemblBacteria; CAC98661; CAC98661; CAC98661.
DR GeneID; 985140; -.
DR KEGG; lmo:lmo0582; -.
DR PATRIC; fig|169963.11.peg.601; -.
DR eggNOG; COG0791; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG3103; Bacteria.
DR HOGENOM; CLU_581142_0_0_9; -.
DR PhylomeDB; P21171; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 2.
DR Gene3D; 3.10.350.10; -; 2.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003646; SH3-like_bac-type.
DR Pfam; PF01476; LysM; 2.
DR Pfam; PF00877; NLPC_P60; 1.
DR Pfam; PF08239; SH3_3; 1.
DR SMART; SM00257; LysM; 2.
DR SMART; SM00287; SH3b; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54106; SSF54106; 2.
DR PROSITE; PS51782; LYSM; 2.
DR PROSITE; PS51935; NLPC_P60; 1.
DR PROSITE; PS51781; SH3B; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Protease; Reference proteome; Repeat;
KW Secreted; Signal; Thiol protease.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:2111287"
FT CHAIN 28..484
FT /note="Probable endopeptidase p60"
FT /id="PRO_0000019760"
FT DOMAIN 28..71
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 80..144
FT /note="SH3b"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
FT DOMAIN 201..244
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 366..484
FT /note="NlpC/P60"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT REGION 150..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..355
FT /note="19 X 2 AA tandem repeats of T-N"
FT COMPBIAS 150..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 396
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 446
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT VARIANT 94
FT /note="S -> T (in strain: Mackaness)"
FT VARIANT 167
FT /note="A -> V (in strain: Mackaness)"
FT VARIANT 196
FT /note="V -> I (in strain: Mackaness)"
FT VARIANT 326..331
FT /note="Missing (in strain: Mackaness)"
SQ SEQUENCE 484 AA; 50587 MW; 3CC0F90591E14E0F CRC64;
MNMKKATIAA TAGIAVTAFA APTIASASTV VVEAGDTLWG IAQSKGTTVD AIKKANNLTT
DKIVPGQKLQ VNNEVAAAEK TEKSVSATWL NVRSGAGVDN SIITSIKGGT KVTVETTESN
GWHKITYNDG KTGFVNGKYL TDKAVSTPVA PTQEVKKETT TQQAAPAAET KTEVKQTTQA
TTPAPKVAET KETPVVDQNA TTHAVKSGDT IWALSVKYGV SVQDIMSWNN LSSSSIYVGQ
KLAIKQTANT ATPKAEVKTE APAAEKQAAP VVKENTNTNT ATTEKKETAT QQQTAPKAPT
EAAKPAPAPS TNTNANKTNT NTNTNTNTNN TNTNTPSKNT NTNSNTNTNT NSNTNANQGS
SNNNSNSSAS AIIAEAQKHL GKAYSWGGNG PTTFDCSGYT KYVFAKAGIS LPRTSGAQYA
STTRISESQA KPGDLVFFDY GSGISHVGIY VGNGQMINAQ DNGVKYDNIH GSGWGKYLVG
FGRV
