INLJ_LISMO
ID INLJ_LISMO Reviewed; 851 AA.
AC Q8Y3L4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Internalin J {ECO:0000303|PubMed:16177371};
DE Flags: Precursor;
GN Name=inlJ; OrderedLocusNames=lmo2821;
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 FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e, and CLIP 80459 / Serotype 4b;
RX PubMed=16177371; DOI=10.1128/iai.73.10.6912-6922.2005;
RA Sabet C., Lecuit M., Cabanes D., Cossart P., Bierne H.;
RT "LPXTG protein InlJ, a newly identified internalin involved in Listeria
RT monocytogenes virulence.";
RL Infect. Immun. 73:6912-6922(2005).
RN [3]
RP INTERACTION WITH HUMAN MUC2, SUBUNIT, AND DOMAIN.
RX PubMed=18327567; DOI=10.1007/s00203-008-0358-6;
RA Linden S.K., Bierne H., Sabet C., Png C.W., Florin T.H., McGuckin M.A.,
RA Cossart P.;
RT "Listeria monocytogenes internalins bind to the human intestinal mucin
RT MUC2.";
RL Arch. Microbiol. 190:101-104(2008).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, INDUCTION, CELL WALL
RP ANCHORING BY SRTA, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=18227172; DOI=10.1128/iai.01519-07;
RA Sabet C., Toledo-Arana A., Personnic N., Lecuit M., Dubrac S., Poupel O.,
RA Gouin E., Nahori M.A., Cossart P., Bierne H.;
RT "The Listeria monocytogenes virulence factor InlJ is specifically expressed
RT in vivo and behaves as an adhesin.";
RL Infect. Immun. 76:1368-1378(2008).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=21725001; DOI=10.1128/jb.01154-10;
RA Bruck S., Personnic N., Prevost M.C., Cossart P., Bierne H.;
RT "Regulated shift from helical to polar localization of Listeria
RT monocytogenes cell wall-anchored proteins.";
RL J. Bacteriol. 193:4425-4437(2011).
RN [6] {ECO:0007744|PDB:3BZ5}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 52-508, AND LRR REPEATS.
RX PubMed=18343406; DOI=10.1016/j.jmb.2008.01.100;
RA Bublitz M., Holland C., Sabet C., Reichelt J., Cossart P., Heinz D.W.,
RA Bierne H., Schubert W.D.;
RT "Crystal structure and standardized geometric analysis of InlJ, a listerial
RT virulence factor and leucine-rich repeat protein with a novel cysteine
RT ladder.";
RL J. Mol. Biol. 378:87-96(2008).
CC -!- FUNCTION: Involved in several steps of L.monocytogenes infection by
CC both intravenous and oral infection (PubMed:16177371). Probably acts as
CC an adhesion; upon ectopic expression in L.innocula bacteria adhere
CC better to human cell lines (PubMed:18227172).
CC {ECO:0000269|PubMed:16177371, ECO:0000269|PubMed:18227172}.
CC -!- ACTIVITY REGULATION: Despite being transcribed during bacterial growth
CC in culture the protein is only detected in infected mice.
CC {ECO:0000269|PubMed:18227172}.
CC -!- SUBUNIT: Nearly full-length mature protein and an internal LRR-
CC containing fragment interact in vitro with human intestinal mucin-2
CC (MUC2) but not with mucin-1. LRR fragment binding is slightly better at
CC pH 5.5, (the pH of the intestine) than at pH 7.4.
CC {ECO:0000269|PubMed:18327567}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477, ECO:0000269|PubMed:18227172,
CC ECO:0000269|PubMed:21725001}; Peptidoglycan-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00477}. Note=No protein is expressed
CC when grown in liquid culture; protein is detected 72 hours post-
CC inoculation in intravenously infected mice (PubMed:18227172). Upon
CC expression under control of a heterologous promoter during exponential
CC growth is detected on the cell surface as a series of dots in a helical
CC pattern, it is excluded from the septum; at very high expression levels
CC it accumulates at cell poles (PubMed:21725001). The helical pattern of
CC InlA does not overlap with that of InlH, InlJ or Hbp2 (SvpA)
CC (PubMed:21725001). In stationary phase remains outside of the cell pole
CC and septum (PubMed:21725001). {ECO:0000269|PubMed:18227172,
CC ECO:0000269|PubMed:21725001}.
CC -!- INDUCTION: Expressed in late exponential phase.
CC {ECO:0000269|PubMed:16177371}.
CC -!- DOMAIN: The LRR domain (34-508) binds more efficiently in vitro to
CC human intestinal mucin-2 (MUC2) than does a nearly whole protein (26-
CC 792) suggesting the MucBP domains do not function in mucin-binding in
CC Listeria. {ECO:0000269|PubMed:18327567}.
CC -!- DISRUPTION PHENOTYPE: No visible effect on colonization of host tissue
CC culture cells; decreased organ colonization in mice.
CC {ECO:0000269|PubMed:16177371, ECO:0000269|PubMed:18227172}.
CC -!- SIMILARITY: Belongs to the internalin family.
CC {ECO:0000305|PubMed:16177371}.
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DR EMBL; AL591984; CAD01034.1; -; Genomic_DNA.
DR PIR; AD1427; AD1427.
DR RefSeq; NP_466343.1; NC_003210.1.
DR RefSeq; WP_010990081.1; NZ_CP023861.1.
DR PDB; 3BZ5; X-ray; 2.70 A; A=52-508.
DR PDBsum; 3BZ5; -.
DR AlphaFoldDB; Q8Y3L4; -.
DR SMR; Q8Y3L4; -.
DR STRING; 169963.lmo2821; -.
DR PaxDb; Q8Y3L4; -.
DR EnsemblBacteria; CAD01034; CAD01034; CAD01034.
DR GeneID; 984504; -.
DR KEGG; lmo:lmo2821; -.
DR PATRIC; fig|169963.11.peg.2892; -.
DR eggNOG; COG4886; Bacteria.
DR eggNOG; COG4932; Bacteria.
DR HOGENOM; CLU_320241_0_0_9; -.
DR OMA; PLNTINC; -.
DR PhylomeDB; Q8Y3L4; -.
DR BioCyc; LMON169963:LMO2821-MON; -.
DR EvolutionaryTrace; Q8Y3L4; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1220; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR009459; MucBP_dom.
DR Pfam; PF06458; MucBP; 4.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell wall; Leucine-rich repeat;
KW Peptidoglycan-anchor; Reference proteome; Repeat; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..824
FT /note="Internalin J"
FT /id="PRO_0000252679"
FT PROPEP 825..851
FT /note="Removed by sortase A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000269|PubMed:18227172"
FT /id="PRO_0000252680"
FT REPEAT 94..115
FT /note="LRR 1"
FT /evidence="ECO:0000269|PubMed:18343406"
FT REPEAT 116..136
FT /note="LRR 2"
FT /evidence="ECO:0000269|PubMed:18343406"
FT REPEAT 137..157
FT /note="LRR 3"
FT /evidence="ECO:0000269|PubMed:18343406"
FT REPEAT 158..179
FT /note="LRR 4"
FT /evidence="ECO:0000269|PubMed:18343406"
FT REPEAT 180..200
FT /note="LRR 5"
FT /evidence="ECO:0000269|PubMed:18343406"
FT REPEAT 201..221
FT /note="LRR 6"
FT /evidence="ECO:0000269|PubMed:18343406"
FT REPEAT 222..243
FT /note="LRR 7"
FT /evidence="ECO:0000269|PubMed:18343406"
FT REPEAT 244..263
FT /note="LRR 8"
FT /evidence="ECO:0000269|PubMed:18343406"
FT REPEAT 264..284
FT /note="LRR 9"
FT /evidence="ECO:0000269|PubMed:18343406"
FT REPEAT 285..306
FT /note="LRR 10"
FT /evidence="ECO:0000269|PubMed:18343406"
FT REPEAT 316..325
FT /note="LRR 11"
FT /evidence="ECO:0000269|PubMed:18343406"
FT REPEAT 338..357
FT /note="LRR 12"
FT /evidence="ECO:0000269|PubMed:18343406"
FT REPEAT 359..368
FT /note="LRR 13"
FT /evidence="ECO:0000269|PubMed:18343406"
FT REPEAT 380..402
FT /note="LRR 14"
FT /evidence="ECO:0000269|PubMed:18343406"
FT DOMAIN 506..568
FT /note="MucBP 1"
FT DOMAIN 576..638
FT /note="MucBP 2"
FT DOMAIN 647..709
FT /note="MucBP 3"
FT DOMAIN 717..779
FT /note="MucBP 4"
FT REGION 786..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 821..825
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 786..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 824
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3BZ5"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:3BZ5"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:3BZ5"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3BZ5"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:3BZ5"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:3BZ5"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 417..426
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 454..464
FT /evidence="ECO:0007829|PDB:3BZ5"
FT TURN 465..468
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 469..474
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:3BZ5"
FT STRAND 491..501
FT /evidence="ECO:0007829|PDB:3BZ5"
SQ SEQUENCE 851 AA; 92803 MW; 7510519A85D53A55 CRC64;
MKTTKIVIAS LVSLTMVSNP LLTFAATNDV IDNTTEITTD KETSSTQPTI KNTLKAGQTQ
SFNDWFPDDN FASEVAAAFE MQATDTISEE QLATLTSLDC HNSSITDMTG IEKLTGLTKL
ICTSNNITTL DLSQNTNLTY LACDSNKLTN LDVTPLTKLT YLNCDTNKLT KLDVSQNPLL
TYLNCARNTL TEIDVSHNTQ LTELDCHLNK KITKLDVTPQ TQLTTLDCSF NKITELDVSQ
NKLLNRLNCD TNNITKLDLN QNIQLTFLDC SSNKLTEIDV TPLTQLTYFD CSVNPLTELD
VSTLSKLTTL HCIQTDLLEI DLTHNTQLIY FQAEGCRKIK ELDVTHNTQL YLLDCQAAGI
TELDLSQNPK LVYLYLNNTE LTELDVSHNT KLKSLSCVNA HIQDFSSVGK IPALNNNFEA
EGQTITMPKE TLTNNSLTIA VSPDLLDQFG NPMNIEPGDG GVYDQATNTI TWENLSTDNP
AVTYTFTSEN GAIVGTVTTP FEAPQPIKGE DVTVHYLDDK GEKLADDEVL SGNLDDPYTS
SAKDIPDYTL TTTPDNATGT FTTTSQSVTY VYTKNIVAAE PVTVNYVDDT GKTLSPSEIL
NGNVGDTYNA TAKQIDGYTL SAEPTNATGQ FTSSAQTVNY IYTKNPAPEK GVVEIHYVDE
DNKQLNSTTE ISGTIGDNYT TEPKTIEGYT LTTTPGNATG TFTTGSQTVT YVYTKNIEAA
EPITVNYVDA NGKTLAPSET LNGNVGDTYK ATAKQIDGYT LSAEPTNATG QFTSSAQTVN
YIYTKNTNTD QPLPTKKPTN TTPTKPSNLK TTEVKKASDT LPKTGDSAPW KSALLGVFLS
STALVIWKKK K
