ID   INLJ_LISMF              Reviewed;         916 AA.
AC   Q71VU0;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Internalin J;
DE   Flags: Precursor;
GN   Name=inlJ; OrderedLocusNames=LMOf2365_2812;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA   Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA   White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA   Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA   Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA   Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA   Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT   pathogen Listeria monocytogenes reveal new insights into the core genome
RT   components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
CC   -!- FUNCTION: Involved in several steps of L.monocytogenes infection,
CC       probably improves adhesin to host cells.
CC       {ECO:0000250|UniProtKB:Q8Y3L4}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}.
CC   -!- SIMILARITY: Belongs to the internalin family. {ECO:0000305}.
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DR   EMBL; AE017262; AAT05576.1; -; Genomic_DNA.
DR   RefSeq; WP_010959113.1; NC_002973.6.
DR   AlphaFoldDB; Q71VU0; -.
DR   SMR; Q71VU0; -.
DR   KEGG; lmf:LMOf2365_2812; -.
DR   HOGENOM; CLU_320241_0_0_9; -.
DR   OMA; PLNTINC; -.
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; 5.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   3: Inferred from homology;
KW   Cell adhesion; Cell wall; Leucine-rich repeat; Peptidoglycan-anchor;
KW   Repeat; Secreted; Signal; Virulence.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..889
FT                   /note="Internalin J"
FT                   /id="PRO_0000252677"
FT   PROPEP          890..916
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000252678"
FT   REPEAT          94..115
FT                   /note="LRR 1"
FT   REPEAT          116..136
FT                   /note="LRR 2"
FT   REPEAT          137..157
FT                   /note="LRR 3"
FT   REPEAT          158..179
FT                   /note="LRR 4"
FT   REPEAT          180..200
FT                   /note="LRR 5"
FT   REPEAT          201..221
FT                   /note="LRR 6"
FT   REPEAT          222..243
FT                   /note="LRR 7"
FT   REPEAT          244..263
FT                   /note="LRR 8"
FT   REPEAT          264..284
FT                   /note="LRR 9"
FT   REPEAT          285..306
FT                   /note="LRR 10"
FT   REPEAT          316..325
FT                   /note="LRR 11"
FT   REPEAT          338..357
FT                   /note="LRR 12"
FT   REPEAT          359..368
FT                   /note="LRR 13"
FT   REPEAT          380..402
FT                   /note="LRR 14"
FT   DOMAIN          506..568
FT                   /note="MucBP 1"
FT   DOMAIN          576..638
FT                   /note="MucBP 2"
FT   DOMAIN          646..708
FT                   /note="MucBP 3"
FT   DOMAIN          717..779
FT                   /note="MucBP 4"
FT   DOMAIN          787..849
FT                   /note="MucBP 5"
FT   REGION          862..888
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           886..890
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        862..880
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         889
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   916 AA;  99557 MW;  EC27B2E69FDA231F CRC64;
     MKTSKIIIAS LVSLTLVSNP ILTFAATNDV IDSTTEITTD KEISSTQPTI KTTLKAGQTQ
     SFNDWFPDDN FASEVAAAFE MQATDTISEE QLATLTSLDC HNSSIADMTG IEKLTGLTKL
     ICTYNNITTL DLSQNTNLTY LACDSNKLTN LDVTPLTKLT YLNCDTNKLT KIDVSQNPLL
     TYLNCARNTL TEIDVSHNTQ LTELDCHLNK KITKLDVTPQ TQLTTLDCSF NKITALDVSQ
     NKLLNRLNCD TNNITKLDLN QNIQLTFLNC SSNKLTEIDV TPLTQLTYFD CSVNPLTELD
     VSTLSKLTTL HCIQTDLLEI DLTHNTQLIY FQAEGCRKIK ELDVTHNTQL YLLDCQAAGI
     TELDLSQNPK LVYLYLNNTE LTKLDVSHNT KLKSLSCVNA HIQDFSSVGK IPVLNNNLDA
     EGQTITMPKE TLTNNSLTIA VSPDLLDQFG NPMNIEPGDG GVYDQATNTI TWENLSTDNP
     AVTYTFTSEN GAIVGTVTTP FEAPQPIKGE DVTVHYLDDK GEKLAADEVL SGNLDDPYTS
     SAKDIPDYTL TTTPDNATGT FTTTSQSVTY VYTKNIVAAE PVTVNYVDDT GKTLAPSETL
     NGNVGDTYNA TAKQIDGYTL STTPNNATGT FNTSSQTVTY VYTKNIVAAE PVTVNYVDDT
     GKTLAPSETL NGNVGDTYNA TAKQIDGYTL SAEPTNATGQ FTSSAQTVNY IYTKNPAPEK
     GVVEIHYVDE NNKQLSSATK ISGTVGDNYT TEPKNIDGYT LTTTPDNATG TFNTSSQTVT
     YVYTKNIVAA EPVTVNYVDA NGKTLAPSET LNGTIGDTYN ATAKQIDGYT LSAEPTNATG
     QFTNSAQTVN YIYTKNTNID QPLPDKKTTK PSNLKTTEVK KASDTLPKTG DSTPWKSALL
     GVFLSSTALV IWKKKK