HBP1_LISMO
ID HBP1_LISMO Reviewed; 207 AA.
AC Q8Y585;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Hemin/hemoglobin-binding protein 1 {ECO:0000303|PubMed:21545655};
DE Short=Hn/Hb-binding protein 1 {ECO:0000303|PubMed:21545655};
DE AltName: Full=Cell wall protein Lmo2186 {ECO:0000305};
DE Flags: Precursor;
GN Name=hbp1 {ECO:0000303|PubMed:21545655}; OrderedLocusNames=lmo2186;
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 PROTEIN SEQUENCE OF 68-176, IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION,
RP AND PROCESSING BY SRTB.
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 SUBCELLULAR LOCATION, PROCESSING BY SRTB, AND MUTAGENESIS OF
RP 170-ASN--THR-173; 175-PRO--SER-178; PRO-175; 176-LYS--SER-178 AND LYS-176.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=19129190; DOI=10.1074/jbc.m807989200;
RA Mariscotti J.F., Garcia-del Portillo F., Pucciarelli M.G.;
RT "The Listeria monocytogenes sortase-B recognizes varied amino acids at
RT position 2 of the sorting motif.";
RL J. Biol. Chem. 284:6140-6146(2009).
RN [4]
RP DISCUSSION OF SEQUENCE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=21545655; DOI=10.1111/j.1365-2958.2011.07667.x;
RA Xiao Q., Jiang X., Moore K.J., Shao Y., Pi H., Dubail I., Charbit A.,
RA Newton S.M., Klebba P.E.;
RT "Sortase independent and dependent systems for acquisition of haem and
RT haemoglobin in Listeria monocytogenes.";
RL Mol. Microbiol. 80:1581-1597(2011).
RN [5]
RP FUNCTION, AND HEMIN AND HEMOGLOBIN-BINDING.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=25315777; DOI=10.1074/jbc.m114.583013;
RA Malmirchegini G.R., Sjodt M., Shnitkind S., Sawaya M.R., Rosinski J.,
RA Newton S.M., Klebba P.E., Clubb R.T.;
RT "Novel mechanism of hemin capture by Hbp2, the hemoglobin-binding hemophore
RT from Listeria monocytogenes.";
RL J. Biol. Chem. 289:34886-34899(2014).
CC -!- FUNCTION: Binds both host hemin and hemoglobin with affinity in the
CC nanomolar range and presumably directs it to membrane transporters.
CC {ECO:0000269|PubMed:25315777}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:16247833,
CC ECO:0000269|PubMed:19129190}; Peptidoglycan-anchor
CC {ECO:0000269|PubMed:16247833, ECO:0000269|PubMed:19129190}. Secreted
CC {ECO:0000269|PubMed:19129190}.
CC -!- INDUCTION: Present in both exponential and stationary phase (at protein
CC level). {ECO:0000269|PubMed:16247833}.
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DR EMBL; AL591982; CAD00264.1; -; Genomic_DNA.
DR PIR; AB1348; AB1348.
DR RefSeq; NP_465710.1; NC_003210.1.
DR RefSeq; WP_003731900.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y585; -.
DR SMR; Q8Y585; -.
DR STRING; 169963.lmo2186; -.
DR PaxDb; Q8Y585; -.
DR EnsemblBacteria; CAD00264; CAD00264; CAD00264.
DR GeneID; 984742; -.
DR KEGG; lmo:lmo2186; -.
DR PATRIC; fig|169963.11.peg.2238; -.
DR eggNOG; COG5386; Bacteria.
DR HOGENOM; CLU_092243_0_1_9; -.
DR OMA; MNRFEQF; -.
DR PhylomeDB; Q8Y585; -.
DR BioCyc; LMON169963:LMO2186-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
DR GO; GO:0030492; F:hemoglobin binding; IEA:InterPro.
DR GO; GO:0071281; P:cellular response to iron ion; IEP:CollecTF.
DR GO; GO:0015886; P:heme transport; IEA:InterPro.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR CDD; cd06920; NEAT; 1.
DR Gene3D; 2.60.40.1850; -; 1.
DR InterPro; IPR019909; Haem_uptake_protein_IsdC.
DR InterPro; IPR006635; NEAT_dom.
DR InterPro; IPR037250; NEAT_dom_sf.
DR InterPro; IPR017502; Sortase_SrtB_target.
DR Pfam; PF05031; NEAT; 1.
DR SMART; SM00725; NEAT; 1.
DR SUPFAM; SSF158911; SSF158911; 1.
DR TIGRFAMs; TIGR03656; IsdC; 1.
DR TIGRFAMs; TIGR03063; srtB_target; 1.
DR PROSITE; PS50978; NEAT; 1.
PE 1: Evidence at protein level;
KW Cell wall; Direct protein sequencing; Ion transport; Iron; Iron transport;
KW Peptidoglycan-anchor; Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..207
FT /note="Hemin/hemoglobin-binding protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004317273"
FT PROPEP 178..207
FT /note="Removed by sortase B"
FT /evidence="ECO:0000269|PubMed:16247833"
FT /id="PRO_0000445905"
FT DOMAIN 29..148
FT /note="NEAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00337"
FT REGION 151..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 174..178
FT /note="NPKXZ sorting signal"
FT /evidence="ECO:0000305|PubMed:16247833"
FT MOD_RES 177
FT /note="Murein peptidoglycan amidated serine"
FT /evidence="ECO:0000305|PubMed:16247833"
FT MUTAGEN 170..173
FT /note="Missing: No change in attachment to the cell wall."
FT /evidence="ECO:0000269|PubMed:19129190"
FT MUTAGEN 175..178
FT /note="Missing: No longer attached to the cell wall."
FT /evidence="ECO:0000269|PubMed:19129190"
FT MUTAGEN 175
FT /note="P->A: No longer attached to the cell wall."
FT /evidence="ECO:0000269|PubMed:19129190"
FT MUTAGEN 176..178
FT /note="KSS->QTN: Attached to the cell wall."
FT /evidence="ECO:0000269|PubMed:19129190"
FT MUTAGEN 176
FT /note="K->Q: Attached to the cell wall."
FT /evidence="ECO:0000269|PubMed:19129190"
SQ SEQUENCE 207 AA; 22267 MW; 037FB996D6010695 CRC64;
MKKVLVFAAF IVLFSFSFLS TGLTAQAALK DGTYSVDYTV IQGDSDSASM ANDYFDKPAT
VTVNGGKSTV SLQVNHSKWI TGLWVEGNAV SVTSKNASSD TRKVSFPVST LSNPVNAKIK
VDIDDDDLNY HHEYQIKLRF DEGSAKALAG AVKSSDNNTT TPATKSDSSN KVTNPKSSDS
SQMFLYGIIF VATGAGLILL KRRAIFK
