HASA_SERMA
ID HASA_SERMA Reviewed; 188 AA.
AC Q54450;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Hemophore HasA;
DE AltName: Full=Heme acquisition system protein A;
GN Name=hasA;
OS Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, FUNCTION,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=SM365;
RX PubMed=7937909; DOI=10.1073/pnas.91.21.9876;
RA Letoffe S., Ghigo J.-M., Wandersman C.;
RT "Iron acquisition from heme and hemoglobin by a Serratia marcescens
RT extracellular protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9876-9880(1994).
RN [2]
RP PROTEIN SEQUENCE, AND SUBUNIT.
RX PubMed=9188703; DOI=10.1021/bi962577s;
RA Izadi N., Henry Y., Haladjian J., Goldberg M.E., Wandersman C.,
RA Delepierre M., Lecroisey A.;
RT "Purification and characterization of an extracellular heme-binding
RT protein, HasA, involved in heme iron acquisition.";
RL Biochemistry 36:7050-7057(1997).
RN [3]
RP FUNCTION.
RC STRAIN=SM365;
RX PubMed=9171402; DOI=10.1128/jb.179.11.3572-3579.1997;
RA Ghigo J.M., Letoffe S., Wandersman C.;
RT "A new type of hemophore-dependent heme acquisition system of Serratia
RT marcescens reconstituted in Escherichia coli.";
RL J. Bacteriol. 179:3572-3579(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=10360351; DOI=10.1038/9281;
RA Arnoux P., Haser R., Izadi N., Lecroisey A., Delepierre M., Wandersman C.,
RA Czjzek M.;
RT "The crystal structure of HasA, a hemophore secreted by Serratia
RT marcescens.";
RL Nat. Struct. Biol. 6:516-520(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS).
RX PubMed=10966573;
RX DOI=10.1002/1097-0134(20001101)41:2<202::aid-prot50>3.0.co;2-8;
RA Arnoux P., Haser R., Izadi-Pruneyre N., Lecroisey A., Czjzek M.;
RT "Functional aspects of the heme bound hemophore HasA by structural analysis
RT of various crystal forms.";
RL Proteins 41:202-210(2000).
CC -!- FUNCTION: Can bind free heme and also acquire it from hemoglobin.
CC Conveys heme from hemoglobin to the HasR receptor which releases it
CC into the bacterium. HasR alone can take up heme but the synergy between
CC HasA and HasR increases heme uptake 100-fold.
CC {ECO:0000269|PubMed:7937909, ECO:0000269|PubMed:9171402}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9188703}.
CC -!- INTERACTION:
CC Q54450; Q79AD2: hasR; NbExp=3; IntAct=EBI-6399956, EBI-6399951;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7937909}.
CC -!- INDUCTION: By iron depletion. {ECO:0000269|PubMed:7937909}.
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DR EMBL; X81195; CAA57068.1; -; Genomic_DNA.
DR PIR; T48671; T48671.
DR RefSeq; WP_016928898.1; NZ_VOUW01000012.1.
DR PDB; 1B2V; X-ray; 1.90 A; A=1-188.
DR PDB; 1DK0; X-ray; 1.77 A; A/B=1-188.
DR PDB; 1DKH; X-ray; 3.20 A; A=1-188.
DR PDB; 1YBJ; NMR; -; A=2-179.
DR PDB; 2CN4; X-ray; 2.30 A; A/B=2-174.
DR PDB; 2UYD; X-ray; 2.70 A; X=1-188.
DR PDB; 3CSL; X-ray; 2.70 A; C/D=2-188.
DR PDB; 3CSN; X-ray; 3.00 A; C/D=2-188.
DR PDB; 3DDR; X-ray; 2.80 A; C/D=2-188.
DR PDB; 5C58; X-ray; 2.79 A; B=2-188.
DR PDBsum; 1B2V; -.
DR PDBsum; 1DK0; -.
DR PDBsum; 1DKH; -.
DR PDBsum; 1YBJ; -.
DR PDBsum; 2CN4; -.
DR PDBsum; 2UYD; -.
DR PDBsum; 3CSL; -.
DR PDBsum; 3CSN; -.
DR PDBsum; 3DDR; -.
DR PDBsum; 5C58; -.
DR AlphaFoldDB; Q54450; -.
DR BMRB; Q54450; -.
DR SMR; Q54450; -.
DR DIP; DIP-48682N; -.
DR IntAct; Q54450; 2.
DR STRING; 273526.SMDB11_0285; -.
DR TCDB; 1.B.14.5.1; the outer membrane receptor (omr) family.
DR PATRIC; fig|615.99.peg.4532; -.
DR EvolutionaryTrace; Q54450; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1500.10; -; 1.
DR InterPro; IPR010495; HasA_haem-bd.
DR InterPro; IPR036912; HasA_haem-bd_sf.
DR Pfam; PF06438; HasA; 1.
DR PIRSF; PIRSF019876; HasA; 1.
DR SUPFAM; SSF54621; SSF54621; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Secreted.
FT CHAIN 1..188
FT /note="Hemophore HasA"
FT /id="PRO_0000083901"
FT BINDING 32
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 75
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT CONFLICT 170
FT /note="A -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1DK0"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1DK0"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:3CSL"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:1DK0"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:2UYD"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1DK0"
FT STRAND 44..58
FT /evidence="ECO:0007829|PDB:1DK0"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1DK0"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:1DK0"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1DK0"
FT STRAND 85..99
FT /evidence="ECO:0007829|PDB:1DK0"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1DK0"
FT STRAND 107..116
FT /evidence="ECO:0007829|PDB:1DK0"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1DK0"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:1DK0"
FT HELIX 131..140
FT /evidence="ECO:0007829|PDB:1DK0"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:1DK0"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1DK0"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:3DDR"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:1DK0"
SQ SEQUENCE 188 AA; 19283 MW; 8E4ACC8DB254FC6D CRC64;
MAFSVNYDSS FGGYSIHDYL GQWASTFGDV NHTNGNVTDA NSGGFYGGSL SGSQYAISST
ANQVTAFVAG GNLTYTLFNE PAHTLYGQLD SLSFGDGLSG GDTSPYSIQV PDVSFGGLNL
SSLQAQGHDG VVHQVVYGLM SGDTGALETA LNGILDDYGL SVNSTFDQVA AATAVGVQHA
DSPELLAA
