HBHA_MYCBO
ID HBHA_MYCBO Reviewed; 199 AA.
AC P0C2T3; A0A1R3XVE5; O85733; P0A5P7; Q11142; X2BF49;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Heparin-binding hemagglutinin;
DE AltName: Full=Adhesin;
GN Name=hbhA; OrderedLocusNames=BQ2027_MB0485;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [3]
RP FUNCTION.
RC STRAIN=BCG;
RX PubMed=11449276; DOI=10.1038/35084083;
RA Pethe K., Alonso S., Biet F., Delogu G., Brennan M.J., Locht C.,
RA Menozzi F.D.;
RT "The heparin-binding haemagglutinin of M. tuberculosis is required for
RT extrapulmonary dissemination.";
RL Nature 412:190-194(2001).
CC -!- FUNCTION: Required for extrapulmonary dissemination. Mediates adherence
CC to epithelial cells by binding to sulfated glycoconjugates present at
CC the surface of these cells; binds heparin, dextran sulfate, fucoidan
CC and chondroitin sulfate. Promotes hemagglutination of erythrocytes of
CC certain host species. Induces mycobacterial aggregation.
CC {ECO:0000269|PubMed:11449276}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250}.
CC -!- PTM: Glycosylated. Glycosylation may protect the protein from
CC proteolytic degradation and be important for hemagglutination. It
CC suggests that the carbohydrate moiety may be located within the C-
CC terminal domain of HbhA (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: To M.leprae HbhA. {ECO:0000305}.
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DR EMBL; LT708304; SIT99080.1; -; Genomic_DNA.
DR RefSeq; NP_854148.1; NC_002945.3.
DR RefSeq; WP_003402339.1; NC_002945.4.
DR AlphaFoldDB; P0C2T3; -.
DR SMR; P0C2T3; -.
DR GeneID; 45424436; -.
DR PATRIC; fig|233413.5.peg.527; -.
DR OMA; RERWANL; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Cell adhesion; Glycoprotein; Hemagglutinin; Heparin-binding; Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..199
FT /note="Heparin-binding hemagglutinin"
FT /id="PRO_0000083908"
FT REGION 162..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..199
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 199 AA; 21534 MW; E9C1C011F8B460ED CRC64;
MAENSNIDDI KAPLLAALGA ADLALATVNE LITNLRERAE ETRTDTRSRV EESRARLTKL
QEDLPEQLTE LREKFTAEEL RKAAEGYLEA ATSRYNELVE RGEAALERLR SQQSFEEVSA
RAEGYVDQAV ELTQEALGTV ASQTRAVGER AAKLVGIELP KKAAPAKKAA PAKKAAPAKK
AAAKKAPAKK AAAKKVTQK
