INLH_LISMO
ID INLH_LISMO Reviewed; 548 AA.
AC Q7AP87;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Internalin H;
DE Flags: Precursor;
GN Name=inlH; OrderedLocusNames=lmo0263;
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 IDENTIFICATION BY MASS SPECTROMETRY, AND PROCESSING BY SRTA.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=16247833; DOI=10.1002/pmic.200402075;
RA Pucciarelli M.G., Calvo E., Sabet C., Bierne H., Cossart P.,
RA Garcia-del Portillo F.;
RT "Identification of substrates of the Listeria monocytogenes sortases A and
RT B by a non-gel proteomic analysis.";
RL Proteomics 5:4808-4817(2005).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY STRESS, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=20176794; DOI=10.1128/iai.01096-09;
RA Personnic N., Bruck S., Nahori M.A., Toledo-Arana A., Nikitas G.,
RA Lecuit M., Dussurget O., Cossart P., Bierne H.;
RT "The stress-induced virulence protein InlH controls interleukin-6
RT production during murine listeriosis.";
RL Infect. Immun. 78:1979-1989(2010).
RN [4]
RP SUBCELLULAR LOCATION, AND INDUCTION.
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 [5]
RP SUBCELLULAR LOCATION, AND PROCESSING BY SRTA.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=22837151; DOI=10.2436/20.1501.01.157;
RA Mariscotti J.F., Quereda J.J., Pucciarelli M.G.;
RT "Contribution of sortase A to the regulation of Listeria monocytogenes
RT LPXTG surface proteins.";
RL Int. Microbiol. 15:43-51(2012).
RN [6] {ECO:0007744|PDB:1H6U}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 37-343, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11575932; DOI=10.1006/jmbi.2001.4989;
RA Schubert W.D., Goebel G., Diepholz M., Darji A., Kloer D., Hain T.,
RA Chakraborty T., Wehland J., Domann E., Heinz D.W.;
RT "Internalins from the human pathogen Listeria monocytogenes combine three
RT distinct folds into a contiguous internalin domain.";
RL J. Mol. Biol. 312:783-794(2001).
CC -!- FUNCTION: Contributes to systemic listeriosis in mice by decreasing
CC host IL-6 cytokine production and thus evasion of the host immune
CC response. Does not contribute to invasion of the host intestinal
CC tissue. {ECO:0000269|PubMed:20176794}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477, ECO:0000269|PubMed:20176794,
CC ECO:0000269|PubMed:21725001, ECO:0000269|PubMed:22837151};
CC Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477,
CC ECO:0000305|PubMed:16247833, ECO:0000305|PubMed:20176794}. Secreted
CC {ECO:0000269|PubMed:22837151}. Note=In the absence of SrtA in
CC exponential phase some protein is still anchored to the cell wall while
CC protein levels are the same in the srtA mutant; in stationary phase
CC much less protein accumulates (PubMed:22837151). During exponential
CC growth detected on the cell surface as a series of dots in a helical
CC pattern, it is excluded from the septum (PubMed:21725001). The helical
CC pattern of InlA does not overlap with that of InlH, InlJ or Hbp2 (SvpA)
CC (PubMed:21725001). In stationary phase colocalizes with InlA at cell
CC poles and at the septum, the location shift requires SigB
CC (PubMed:21725001). {ECO:0000269|PubMed:21725001,
CC ECO:0000269|PubMed:22837151}.
CC -!- INDUCTION: More prevalent in stationary than exponential phase (at
CC protein level) (PubMed:21725001, PubMed:20176794). Single gene
CC transcripts are substantially decreased in a sigB mutant, induced in
CC mouse gut (PubMed:20176794). Induced as cells approach stationary phase
CC and by growth at pH 5.5, at 45 degrees Celsius, in 7.5% NaCl and by
CC oxidative stress (at protein level) (PubMed:20176794, PubMed:21725001).
CC {ECO:0000269|PubMed:20176794, ECO:0000269|PubMed:21725001}.
CC -!- DOMAIN: The N-terminus (36-79) resembles a truncated EF hand, the LRR
CC region (80-262) has a curved form while residues 263-343 form an Ig-
CC like region. {ECO:0000269|PubMed:11575932}.
CC -!- DISRUPTION PHENOTYPE: Increased expression of InlA (PubMed:20176794).
CC No change in invasion or bacterial survival in host mamammalian cells
CC including macrophages (PubMed:20176794). Decreased bacterial counts in
CC blood, spleen and liver of intravenously inoculated BALB/c and C57BL/6
CC mice (PubMed:20176794, PubMed:11575932). Increased production of host
CC IL-6 in liver and spleen of intravenously infected BALB/c mice, but not
CC in macrophage cell lines (PubMed:20176794).
CC {ECO:0000269|PubMed:11575932, ECO:0000269|PubMed:20176794}.
CC -!- SIMILARITY: Belongs to the internalin family. {ECO:0000305}.
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DR EMBL; AL591974; CAD00790.1; -; Genomic_DNA.
DR PIR; AH1107; AH1107.
DR RefSeq; NP_463794.1; NC_003210.1.
DR RefSeq; WP_010989386.1; NZ_CP023861.1.
DR PDB; 1H6U; X-ray; 1.80 A; A=37-343.
DR PDBsum; 1H6U; -.
DR AlphaFoldDB; Q7AP87; -.
DR SMR; Q7AP87; -.
DR STRING; 169963.lmo0263; -.
DR PaxDb; Q7AP87; -.
DR EnsemblBacteria; CAD00790; CAD00790; CAD00790.
DR GeneID; 987355; -.
DR KEGG; lmo:lmo0263; -.
DR PATRIC; fig|169963.11.peg.271; -.
DR eggNOG; COG4886; Bacteria.
DR HOGENOM; CLU_019447_3_0_9; -.
DR OMA; TAINVIF; -.
DR PhylomeDB; Q7AP87; -.
DR BioCyc; LMON169963:LMO0263-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.1220; -; 1.
DR Gene3D; 2.60.40.4270; -; 2.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR024634; Internalin_N.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR013378; Listeria/Bacterioides_rpt.
DR InterPro; IPR042229; Listeria/Bacterioides_rpt_sf.
DR InterPro; IPR012569; LRR-contain_adjacent_dom.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF09479; Flg_new; 2.
DR Pfam; PF12354; Internalin_N; 1.
DR Pfam; PF12799; LRR_4; 2.
DR Pfam; PF08191; LRR_adjacent; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR02543; List_Bact_rpt; 2.
DR PROSITE; PS51450; LRR; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Leucine-rich repeat; Peptidoglycan-anchor;
KW Reference proteome; Repeat; Secreted; Signal; Stress response.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..548
FT /note="Internalin H"
FT /evidence="ECO:0000255"
FT /id="PRO_5004286629"
FT PROPEP 519..548
FT /note="Removed by sortase A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:16247833, ECO:0000305|PubMed:20176794,
FT ECO:0000305|PubMed:22837151"
FT /id="PRO_0000445901"
FT REPEAT 93..105
FT /note="LRR 1"
FT /evidence="ECO:0000269|PubMed:11575932"
FT REPEAT 113..127
FT /note="LRR 2"
FT /evidence="ECO:0000269|PubMed:11575932"
FT REPEAT 135..149
FT /note="LRR 3"
FT /evidence="ECO:0000269|PubMed:11575932"
FT REPEAT 157..171
FT /note="LRR 4"
FT /evidence="ECO:0000269|PubMed:11575932"
FT REPEAT 179..193
FT /note="LRR 5"
FT /evidence="ECO:0000269|PubMed:11575932"
FT REPEAT 201..215
FT /note="LRR 6"
FT /evidence="ECO:0000269|PubMed:11575932"
FT REPEAT 223..236
FT /note="LRR 7"
FT /evidence="ECO:0000269|PubMed:11575932"
FT REGION 480..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 515..519
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT MOD_RES 518
FT /note="Pentaglycyl murein peptidoglycan amidated alanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 548 AA; 58681 MW; 3EE34A05CAA1B88F CRC64;
MKKRWNSVFK LVLMVTAILG LSLYVTTSQG VEVRAESITQ PTAINVIFPD PALANAIKIA
AGKSNVTDTV TQADLDGITT LSAFGTGVTT IEGVQYLNNL IGLELKDNQI TDLTPLKNLT
KITELELSGN PLKNVSAIAG LQSIKTLDLT STQITDVTPL AGLSNLQVLY LDLNQITNIS
PLAGLTNLQY LSIGNAQVSD LTPLANLSKL TTLKADDNKI SDISPLASLP NLIEVHLKNN
QISDVSPLAN TSNLFIVTLT NQTITNQPVF YQNNLVVPNV VKGPSGAPIA PATISDNGTY
ASPNLTWNLT SFINNVSYTF NQSVTFKNTT VPFSGTVTQP LTEAYTAVFD VDGKQTSVTV
GANELIKEPT APTKEGYTFT GWYDAKTGGT KWDFATDKMP AEDITLYAQF TINSYTATFD
IDGKLTTQKV TYQSLLEEPV APTKDGYTFT GWYDAKTGGT KWDFATGKMP AGNITLYAQF
TKNDNPNPDD PTTNTPTGNG DGTSNPSNSG GNTTLPTAGD ENTMLPIFIG VFLLGTATLI
LRKTIKVK
