HBHA_MYCTA
ID HBHA_MYCTA Reviewed; 199 AA.
AC A5TZK3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Heparin-binding hemagglutinin;
DE AltName: Full=Adhesin;
GN Name=hbhA; OrderedLocusNames=MRA_0482;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
RN [2]
RP PROTEIN SEQUENCE OF 2-17, SUBCELLULAR LOCATION, AND CHARACTERIZATION.
RX PubMed=9064359; DOI=10.1084/jem.184.3.993;
RA Menozzi F.D., Rouse J.H., Alavi M., Laude-Sharp M., Muller J., Bischoff R.,
RA Brennan M.J., Locht C.;
RT "Identification of a heparin-binding hemagglutinin present in
RT Mycobacteria.";
RL J. Exp. Med. 184:993-1001(1996).
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 -!- INTERACTION:
CC A5TZK3; A5TZK3: hbhA; NbExp=10; IntAct=EBI-7679697, EBI-7679697;
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:9064359}.
CC -!- DOMAIN: Heparin binding seems to require the C-terminal domain of HbhA.
CC Progressive truncations from the C-terminal end diminish the affinity
CC for heparin (By similarity). {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; CP000611; ABQ72203.1; -; Genomic_DNA.
DR RefSeq; WP_003402339.1; NZ_CP016972.1.
DR AlphaFoldDB; A5TZK3; -.
DR SMR; A5TZK3; -.
DR MINT; A5TZK3; -.
DR STRING; 419947.MRA_0482; -.
DR EnsemblBacteria; ABQ72203; ABQ72203; MRA_0482.
DR GeneID; 45424436; -.
DR KEGG; mra:MRA_0482; -.
DR eggNOG; ENOG50335M1; Bacteria.
DR HOGENOM; CLU_089817_1_0_11; -.
DR OMA; RERWANL; -.
DR OrthoDB; 1643794at2; -.
DR Proteomes; UP000001988; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cell adhesion; Direct protein sequencing; Glycoprotein; Hemagglutinin;
KW Heparin-binding; Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9064359"
FT CHAIN 2..199
FT /note="Heparin-binding hemagglutinin"
FT /id="PRO_0000306418"
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
