ID   INLI_LISMO              Reviewed;        1778 AA.
AC   Q8YA32;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Internalin I {ECO:0000303|PubMed:16177371};
DE   Flags: Precursor;
GN   Name=inlI; OrderedLocusNames=lmo0333;
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   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).
CC   -!- FUNCTION: A role in virulence could not be demonstrated.
CC       {ECO:0000269|PubMed:16177371}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}.
CC   -!- INDUCTION: Expressed in late exponential phase.
CC       {ECO:0000269|PubMed:16177371}.
CC   -!- DISRUPTION PHENOTYPE: No visible effect on colonization of host tissue
CC       culture cells; no change in organ colonization in mice.
CC       {ECO:0000269|PubMed:16177371}.
CC   -!- SIMILARITY: Belongs to the internalin family.
CC       {ECO:0000305|PubMed:16177371}.
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DR   EMBL; AL591975; CAC98412.1; -; Genomic_DNA.
DR   PIR; AF1116; AF1116.
DR   RefSeq; NP_463863.1; NC_003210.1.
DR   RefSeq; WP_010989427.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8YA32; -.
DR   SMR; Q8YA32; -.
DR   STRING; 169963.lmo0333; -.
DR   PaxDb; Q8YA32; -.
DR   EnsemblBacteria; CAC98412; CAC98412; CAC98412.
DR   GeneID; 987568; -.
DR   KEGG; lmo:lmo0333; -.
DR   PATRIC; fig|169963.11.peg.342; -.
DR   eggNOG; COG4886; Bacteria.
DR   eggNOG; COG4932; Bacteria.
DR   HOGENOM; CLU_241292_0_0_9; -.
DR   OMA; SAQGCNI; -.
DR   PhylomeDB; Q8YA32; -.
DR   BioCyc; LMON169963:LMO0333-MON; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 8.
DR   Gene3D; 2.60.40.1220; -; 1.
DR   Gene3D; 3.80.10.10; -; 3.
DR   InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR044056; InlI_Ig-like.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR025875; Leu-rich_rpt_4.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR012569; LRR-contain_adjacent_dom.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR009459; MucBP_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   Pfam; PF18981; InlK_D3; 8.
DR   Pfam; PF12799; LRR_4; 3.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08191; LRR_adjacent; 1.
DR   Pfam; PF06458; MucBP; 3.
DR   SMART; SM00369; LRR_TYP; 12.
DR   SUPFAM; SSF49299; SSF49299; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR   PROSITE; PS51450; LRR; 24.
PE   2: Evidence at transcript level;
KW   Cell wall; Leucine-rich repeat; Peptidoglycan-anchor; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..1746
FT                   /note="Internalin I"
FT                   /id="PRO_0000252675"
FT   PROPEP          1747..1778
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000252676"
FT   REPEAT          155..179
FT                   /note="LRR 1"
FT   REPEAT          183..204
FT                   /note="LRR 2"
FT   REPEAT          205..227
FT                   /note="LRR 3"
FT   REPEAT          228..250
FT                   /note="LRR 4"
FT   REPEAT          251..272
FT                   /note="LRR 5"
FT   REPEAT          277..298
FT                   /note="LRR 6"
FT   REPEAT          299..321
FT                   /note="LRR 7"
FT   REPEAT          322..344
FT                   /note="LRR 8"
FT   REPEAT          345..367
FT                   /note="LRR 9"
FT   REPEAT          368..389
FT                   /note="LRR 10"
FT   REPEAT          390..412
FT                   /note="LRR 11"
FT   REPEAT          413..434
FT                   /note="LRR 12"
FT   REPEAT          435..456
FT                   /note="LRR 13"
FT   REPEAT          457..478
FT                   /note="LRR 14"
FT   REPEAT          479..500
FT                   /note="LRR 15"
FT   REPEAT          501..522
FT                   /note="LRR 16"
FT   REPEAT          523..544
FT                   /note="LRR 17"
FT   REPEAT          545..566
FT                   /note="LRR 18"
FT   REPEAT          567..588
FT                   /note="LRR 19"
FT   REPEAT          589..610
FT                   /note="LRR 20"
FT   REPEAT          611..632
FT                   /note="LRR 21"
FT   REPEAT          633..653
FT                   /note="LRR 22"
FT   REPEAT          657..678
FT                   /note="LRR 23"
FT   REPEAT          685..707
FT                   /note="LRR 24"
FT   REPEAT          708..729
FT                   /note="LRR 25"
FT   REPEAT          730..751
FT                   /note="LRR 26"
FT   REPEAT          752..773
FT                   /note="LRR 27"
FT   DOMAIN          785..872
FT                   /note="LRRCT"
FT   DOMAIN          1510..1569
FT                   /note="MucBP 1"
FT   DOMAIN          1575..1634
FT                   /note="MucBP 2"
FT   DOMAIN          1644..1705
FT                   /note="MucBP 3"
FT   REGION          36..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1716..1742
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1743..1747
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        62..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1725..1742
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1746
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   1778 AA;  191648 MW;  CC1D590BEB38B7DD CRC64;
     MKKKFSIVII SVLLLGYLAP FDTLLVGADE TTVSEDTAVK TAEADSATEG IESETGSDDE
     TAEEPKEAKE AEASKETTEK EEKAKTEEPA SNIKTEINTD KSQLKQTSLK AAVPAGSTYN
     SLFPDDNLAK KLAVIITGNA AATGNESVDS AALLAISQLD LSGETGNDPT DISNIEGLQY
     LENLTSLNLS ENNISDLAPL KDLVNLVSLN LSSNRTLVNL SGVEDLVNLQ ELNVSANKAL
     EDISQVASLP VLKEISAQGC NIKTLELKNP AGAVLPELET FYLQENDLTN LTSLAKLPKL
     KNLYIKGNAS LKSLETLNGA TKLQLIDASN CTDLETLGDI SGLSELEMIQ LSGCSKLKEI
     TSLKNLPNLV NITADSCAIE DLGTLNNLPK LQTLVLSDNE NLTNITAITD LPQLKTLTLD
     GCGITSIGTL DNLPKLEKLD LKENQITSIS EITDLPRLSY LDVSVNNLTT IGDLKKLPLL
     EWLNVSSNRL SDVSTLTNFP SLNYINISNN VIRTVGKMTE LPSLKEFYAQ NNSISDISMI
     HDMPNLRKVD ASNNLITNIG TFDNLPKLQS LDVHSNRITS TSVIHDLPSL ETFNAQTNLI
     TNIGTMDNLP DLTYVNLSFN RIPSLAPIGD LPNLETLIVS DNNSYLRSLG TMDGVPKLRI
     LDLQNNYLNY TGTEGNLSSL SDLTNLTELN LRNNVYIDDI SGLSTLSRLI YLNLDSNKIE
     DISALSNLTN LQELTLENNK IENISALSDL ENLNKLVVSK NKIIDISPVA NMVNRGAIVT
     ASNQTYTLPT VLSYQSSFTI DNPVIWYDGT LLAPSSIGNS GNYKDGKITW TNMTATSSST
     LFNFNRLKDG LTFSGTVTQP YKSAAKVTAD AEQTYTIGDT ISEEQFLKDV NAKSSDGAPV
     TSDFATVVDL NTFGEYEVTL TSEKDGIQGD SCKVIVKVLH GAPVISADQT ISYDKHATIT
     EKQFLEDIHA STDLDTAITT NFSTAVNLNK GGDYTVALNS ENEDGVKAET VYVTVTVNKD
     PAPIISAKTE ITYDKFSKKT EAAFLDDIDA DTNDGSIVTS NFATAVNLDK AGDYTVTLNS
     INSDGVAGTP TAIIVHVEKE KIATISTNTA QQYEKYAKIN ETQFLKDVHA SINASPTTAV
     LESDFETVVK LDVPGTYTVT ITATNEDGGV SAPKEVSVIV RKIPAPEITA DKEITYPKFD
     EVSEAEFLND IHATISDKNV AITSNFSTDV NLNKAGDYTV TLNATNEDGV KATPVEVIVH
     VQQGERPVIT ADATISYDKF ANITEAKFLE DIHATSSDGQ SSTVITSNFQ TATNFKTAMS
     YTVTLNAVNE DGISAEPVAV TVTINKEPAA ALKADAEVSY AKNEAVTESD FFKDVHLEGT
     EAPSTAKATS NFDSVVDRSK TGDYTVTINA TNEDGAVSTP IEVIVHIEAE SAPVITANAE
     VKYNKHEQTD ERRFLYDSEA KIDEANVEIK TDFAEKVDIN KVGTYTVTLT ATNEDGQAAN
     PVEVSVIVSD AAAEKVNVKY VDENGSEISA AETLTGNLDE TFSIDAKSIA GYKCDATLSG
     VFSTVEQTVV FHYKAIKPGV VTIKYEDTNG KAVDEDKQIT GEVGDDFEAE AQTVSGYSCR
     AIASGKITEE PQTITFTYST ATPSKKSGEI TVQYVDESGK KLADSKKVTG NIDDSYSVEA
     KAIEGYSVVG DDSAKGVFTE KSQTVTFKYK KNTQVSKDDP KVKGKTNQPS STDTKLKVDN
     NSLPATGDTE NMILAVLIGF NMLIVASIFL FRKPKTNQ