Y880_LISMO
ID Y880_LISMO Reviewed; 462 AA.
AC Q8Y8L7;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cell wall protein Lmo0880 {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=lmo0880;
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 [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 [2]
RP PROTEIN SEQUENCE OF 155-166; 236-250 AND 283-295, PROCESSING BY SRTA, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11929538; DOI=10.1046/j.1365-2958.2002.02798.x;
RA Bierne H., Mazmanian S.K., Trost M., Pucciarelli M.G., Liu G., Dehoux P.,
RA Jansch L., Garcia-del Portillo F., Schneewind O., Cossart P.;
RT "Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring
RT of surface proteins and affects virulence.";
RL Mol. Microbiol. 43:869-881(2002).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, AND PPROCESSING BY SRTA.
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 [4]
RP SUBCELLULAR LOCATION, AND PROCESSING BY SRTA.
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 -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477, ECO:0000269|PubMed:11929538,
CC ECO:0000269|PubMed:16247833, ECO:0000269|PubMed:22837151};
CC Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477,
CC ECO:0000269|PubMed:11929538, ECO:0000269|PubMed:16247833}. Note=In the
CC absence of SrtA in exponential phase a very small amount is secreted
CC while protein levels decrease in the srtA mutant, suggesting post-
CC transcriptional regulation that involves SrtA. In stationary phase
CC almost no protein accumulates. {ECO:0000269|PubMed:22837151}.
CC -!- INDUCTION: More prevalent in stationary than exponential phase (at
CC protein level). {ECO:0000269|PubMed:16247833}.
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DR EMBL; AL591977; CAC98958.1; -; Genomic_DNA.
DR PIR; AH1184; AH1184.
DR RefSeq; NP_464406.1; NC_003210.1.
DR RefSeq; WP_010989604.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y8L7; -.
DR SMR; Q8Y8L7; -.
DR STRING; 169963.lmo0880; -.
DR PaxDb; Q8Y8L7; -.
DR EnsemblBacteria; CAC98958; CAC98958; CAC98958.
DR GeneID; 986636; -.
DR KEGG; lmo:lmo0880; -.
DR PATRIC; fig|169963.11.peg.905; -.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG4932; Bacteria.
DR HOGENOM; CLU_591610_0_0_9; -.
DR OMA; SLFYNAT; -.
DR PhylomeDB; Q8Y8L7; -.
DR BioCyc; LMON169963:LMO0880-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005518; F:collagen binding; IEA:InterPro.
DR GO; GO:0008932; F:lytic endotransglycosylase activity; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 2.60.40.1280; -; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR008456; Collagen-bd_dom.
DR InterPro; IPR011252; Fibrogen-bd_dom1.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR041171; SDR_Ig.
DR Pfam; PF17961; Big_8; 1.
DR Pfam; PF05737; Collagen_bind; 1.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF49401; SSF49401; 2.
DR SUPFAM; SSF54106; SSF54106; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 1: Evidence at protein level;
KW Cell wall; Direct protein sequencing; Peptidoglycan-anchor;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..462
FT /note="Cell wall protein Lmo0880"
FT /evidence="ECO:0000255"
FT /id="PRO_5004316618"
FT PROPEP 437..462
FT /note="Removed by sortase A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000269|PubMed:11929538, ECO:0000305|PubMed:16247833,
FT ECO:0000305|PubMed:22837151"
FT /id="PRO_0000445903"
FT DOMAIN 356..399
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT MOTIF 433..437
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT MOD_RES 436
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:11929538"
SQ SEQUENCE 462 AA; 49878 MW; D94D4217F42567C6 CRC64;
MKKRWLVFAI ICLIITGFLS PKAEAATDYG SSFFTNVSLQ NQNGEQATNF KENSKVRVAY
DFVITQPVAS GETMTLTIPD QLKLINYGGF PLMDSQGNTI ANATIDQVTG TITLTFTDYV
NTHTDLSGSL FYNATFNSKN IQTDQVNPIA FPVKNTTQTV TPYISKVNSG GGTGSPTIVF
KQGRMDDKDL SILHWTVTLN NALTPIDNAV YTDTLGSGQN LLGSATIKYR DANKKVIATN
IQPIALDADR NFELSIGALN NQSVVITYDT KITTKQKSYT NKATLSGDNL DAVSRNATVN
DYGSGGQGTG TPPAPPVKEE PPFIPAEKQP IEKTVETDFG PLEIVKDSEQ NGKIKVIYKV
KDGDTLPGVA NKFDVSVAEI KDWNNLTSDT LQAGQKLQLT IEKTLLSKIT VPPVQKVTST
TRVDGVVKAT GVLPHTGDSN PFIPFVTGLS LIALGFTFGR KS
