INLI_LISMF
ID INLI_LISMF Reviewed; 1775 AA.
AC Q723X5;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Internalin I;
DE Flags: Precursor;
GN Name=inlI; OrderedLocusNames=LMOf2365_0350;
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: A role in virulence could not be demonstrated.
CC {ECO:0000250|UniProtKB:Q8YA32}.
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; AAT03136.1; -; Genomic_DNA.
DR RefSeq; WP_003724263.1; NC_002973.6.
DR AlphaFoldDB; Q723X5; -.
DR SMR; Q723X5; -.
DR KEGG; lmf:LMOf2365_0350; -.
DR HOGENOM; CLU_241292_0_0_9; -.
DR OMA; SAQGCNI; -.
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; -; 4.
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; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08191; LRR_adjacent; 1.
DR Pfam; PF06458; MucBP; 3.
DR SMART; SM00369; LRR_TYP; 11.
DR SUPFAM; SSF49299; SSF49299; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR PROSITE; PS51450; LRR; 23.
PE 3: Inferred from homology;
KW Cell wall; Leucine-rich repeat; Peptidoglycan-anchor; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1743
FT /note="Internalin I"
FT /id="PRO_0000252673"
FT PROPEP 1744..1775
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000252674"
FT REPEAT 152..176
FT /note="LRR 1"
FT REPEAT 180..201
FT /note="LRR 2"
FT REPEAT 202..224
FT /note="LRR 3"
FT REPEAT 225..247
FT /note="LRR 4"
FT REPEAT 248..269
FT /note="LRR 5"
FT REPEAT 274..295
FT /note="LRR 6"
FT REPEAT 296..318
FT /note="LRR 7"
FT REPEAT 319..341
FT /note="LRR 8"
FT REPEAT 342..364
FT /note="LRR 9"
FT REPEAT 365..386
FT /note="LRR 10"
FT REPEAT 387..409
FT /note="LRR 11"
FT REPEAT 410..431
FT /note="LRR 12"
FT REPEAT 432..453
FT /note="LRR 13"
FT REPEAT 454..475
FT /note="LRR 14"
FT REPEAT 476..497
FT /note="LRR 15"
FT REPEAT 498..519
FT /note="LRR 16"
FT REPEAT 520..541
FT /note="LRR 17"
FT REPEAT 542..563
FT /note="LRR 18"
FT REPEAT 564..585
FT /note="LRR 19"
FT REPEAT 586..607
FT /note="LRR 20"
FT REPEAT 608..629
FT /note="LRR 21"
FT REPEAT 630..650
FT /note="LRR 22"
FT REPEAT 654..675
FT /note="LRR 23"
FT REPEAT 682..704
FT /note="LRR 24"
FT REPEAT 705..726
FT /note="LRR 25"
FT REPEAT 727..748
FT /note="LRR 26"
FT REPEAT 749..770
FT /note="LRR 27"
FT DOMAIN 782..869
FT /note="LRRCT"
FT DOMAIN 1507..1566
FT /note="MucBP 1"
FT DOMAIN 1572..1631
FT /note="MucBP 2"
FT DOMAIN 1641..1702
FT /note="MucBP 3"
FT REGION 36..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1713..1737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1740..1744
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 36..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1743
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1775 AA; 191295 MW; 2D8052CF7A4C4443 CRC64;
MKKKFSIVII SVLLLGYLAP FDTLLVGADE TTVTEDTTVK TAETETATEA TESESGSDNE
KAEEPKEAEA SKETTEKEEK AKTKEPASNI KTEINTDKSQ LKQTNLKAVV PAGSTYNSLF
PDDNLAKKLA VIITGNAAAT GNESVDSAAL LAISQLDLSG ETGNDPTDIS NIEGLQYLEN
LTSLNLSENN ISDLAPIKDL VNLVSLNLSS NRTLVNLSGV EGLVNLQELN VSANKALEDI
SQVAALPVLK EISAQGCNIK TLELDNPAGA ILPELETFYL QENDLTDLTS LAKLPKLKNL
YIKGNASLKS LATLKGATKL QLIDASNCTD LETLGDISGL SELEMIQLSG CSKLKEITSL
KDLPNLVNIT ADSCAIEDLG TLNNLPKLQT LILSDNKDLT NINAITDMPQ LKTLALDGCG
ITSIGTLDNL PKLEKLDLKE NQLTSISEIN DLPRLSYLDV SVNYLTTIGE LKKLPLLEWL
NVSSNRLSDV STLTNFPSLN YINVSNNVIR TVGKMTELPS LKEFYAQNNN VSDISMIHDM
PNLRKVDASN NLITNIGTFD NLPKLQNLDV HSNRITNTSV IHDLPSLETF YAQNNLITNI
GTMDNLPELT YVDLSFNRIP SLAPIGDLPK LEILKVTDNY SYLRSLGTMD GVSKLRNLEL
QNNYLNYTGT EGNLSALSDL TNLTELNLRD NGYISDISGL STLSRLIYLN LDSNKIKDIS
ALSNLTTLQE LTLENNQIED ISALSDLDNL NKLALSKNKI IDISPAANMV NRGASVTASN
QTYTLPTVLS YQSSFTIDNP VVWYDGTPLA PSSIAHSGTY KDGEITWTNM TAASSSTEFN
FNRLKDGLTF SGTITQPYKS AVKVTANAEQ TYTIGDTISE EQFLKDVNAK SSDGAPVTSD
FATVVDLNTF GEYEVTLTSE KDGIQGDSCK VIVKVLHGAP VISADQTINY DKHATITEKQ
FLEDVHASTD LNTAITTNFS TAVNLNKGGD YTVALNSENE DGVKAETVYV TVTVDKDPAP
IISAKTDITY DKFSKKTEAA FLDDIDADTN DGSIITSNFA TAVNLDKAGD YTVTLNSINS
DGVASTPTAI IVHVEKEKIA TISANTAQQY EKYAEINETQ FLKDVHASIN ASPTTAVLES
DFETVVKLDV PGTYTVTITA TNEDGGVSAP KEVSVIVKKL PAPEITADKE ITYPKFDEVS
EAEFLSDIHA TINEKNVTIT SNFSADVNLN KAGDYTVTLN ATNEDGVKAT PVEVIVHVQQ
GERPVITADA TISYDKFANI TEAKFLEDIH ATSSDGQSST VITSNFETAT NFKTAMSYTV
TLNAVNEDGI SAEPVAVTVT INKEPAATLK ADAEVSYAKN EAVTESDFFK DVHLEGAEAP
STAKATSNFD SVVDRSKTGD YTVTINATNE DGAVSTPIEV IVHIGAESAP VITANAEVKY
NKHEQTDERR FLYDSDAKID EANVEIKTDF AEKVDINKVG TYTVTLTATN EDGQAANPVE
VSVIVSDAAA EKVNVKYVDE NGAEISAAET LTGNLDDAFS IDAKSIAGYK CDATLSGVFS
TVEQTVVFHY KAIEPGVVTI KYEDANGKAV AEDKQITGEV GDDFEAEAQT VSGYSCRAIA
SGKITEEPQT ITFTYTTATP SKKSGEITVQ YVDESGKKLA DSKKVTGDID DSYSVEAKAI
DGYSVVGDDS AKGVFTEKSQ TVTFKYKKNT QVSKDEPKVK GKTNQPPSAD TKLKVDNNTL
PATGDTENMA LAVLIGFNML LVASIFLFRK PKTNQ