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 27-MAR-2024, entry version 119.
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; Bacillota; 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.gene:17592984; -.
DR PaxDb; 169963-lmo0333; -.
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 OrthoDB; 2366125at2; -.
DR PhylomeDB; Q8YA32; -.
DR BioCyc; LMON169963:LMO0333-MONOMER; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1220; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 8.
DR Gene3D; 3.10.20.320; Putative peptidoglycan bound protein (lpxtg motif); 3.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR012569; Inl_IR.
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; IPR032675; LRR_dom_sf.
DR InterPro; IPR009459; MucBP_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR NCBIfam; NF033932; LapB_rpt_80; 8.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR46652; LEUCINE-RICH REPEAT AND IQ DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR46652:SF3; LEUCINE-RICH REPEAT-CONTAINING PROTEIN 9 ISOFORM X1; 1.
DR Pfam; PF18981; InlK_D3; 8.
DR Pfam; PF12799; LRR_4; 2.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08191; LRR_adjacent; 1.
DR Pfam; PF06458; MucBP; 3.
DR SMART; SM00364; LRR_BAC; 14.
DR SMART; SM00365; LRR_SD22; 13.
DR SMART; SM00369; LRR_TYP; 12.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52058; L domain-like; 3.
DR SUPFAM; SSF49299; PKD domain; 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
//
