HLYA_PROMI
ID HLYA_PROMI Reviewed; 1577 AA.
AC P16466;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Hemolysin;
DE Flags: Precursor;
GN Name=hpmA;
OS Proteus mirabilis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=584;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 30-43.
RC STRAIN=Isolate 477-12;
RX PubMed=2407716; DOI=10.1128/jb.172.3.1206-1216.1990;
RA Uphoff T.S., Welch R.A.;
RT "Nucleotide sequencing of the Proteus mirabilis calcium-independent
RT hemolysin genes (hpmA and hpmB) reveals sequence similarity with the
RT Serratia marcescens hemolysin genes (shlA and shlB).";
RL J. Bacteriol. 172:1206-1216(1990).
CC -!- FUNCTION: Bacterial hemolysins are exotoxins that attack blood cell
CC membranes and cause cell rupture by mechanisms not clearly defined.
CC -!- FUNCTION: Cell-bound hemolysin, which releases heme-iron from
CC erythrocytes by interaction with the erythrocyte membrane. HpmA
CC requires HpmB function.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane.
CC -!- MISCELLANEOUS: The conserved amphipathic domains in ShlA and HpmA may
CC be responsible for pore formation.
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DR EMBL; M30186; AAA25657.1; -; Genomic_DNA.
DR PIR; A35140; A35140.
DR PDB; 3FY3; X-ray; 1.80 A; A=30-265.
DR PDB; 4W8Q; X-ray; 1.43 A; A=30-265.
DR PDB; 4W8R; X-ray; 1.52 A; A=30-263.
DR PDB; 4W8S; X-ray; 1.51 A; A=30-263.
DR PDB; 4W8T; X-ray; 1.54 A; A=30-263.
DR PDB; 5KDK; X-ray; 2.00 A; A=30-265.
DR PDB; 5KEH; X-ray; 1.55 A; A=30-265.
DR PDB; 5KF3; X-ray; 2.20 A; A=30-265.
DR PDB; 5KKD; X-ray; 2.13 A; A/B=30-265.
DR PDB; 5SZ8; X-ray; 1.83 A; A/B=30-234.
DR PDB; 6PYK; X-ray; 1.35 A; A=30-265.
DR PDB; 6PZL; X-ray; 1.17 A; A=30-265.
DR PDB; 6Q0P; X-ray; 1.54 A; A=30-265.
DR PDBsum; 3FY3; -.
DR PDBsum; 4W8Q; -.
DR PDBsum; 4W8R; -.
DR PDBsum; 4W8S; -.
DR PDBsum; 4W8T; -.
DR PDBsum; 5KDK; -.
DR PDBsum; 5KEH; -.
DR PDBsum; 5KF3; -.
DR PDBsum; 5KKD; -.
DR PDBsum; 5SZ8; -.
DR PDBsum; 6PYK; -.
DR PDBsum; 6PZL; -.
DR PDBsum; 6Q0P; -.
DR AlphaFoldDB; P16466; -.
DR SMR; P16466; -.
DR STRING; 584.AOUC001_04490; -.
DR EvolutionaryTrace; P16466; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR008638; Filamn_hemagglutn_N.
DR InterPro; IPR025157; Hemagglutinin_rpt.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF13332; Fil_haemagg_2; 6.
DR Pfam; PF05860; Haemagg_act; 1.
DR SMART; SM00912; Haemagg_act; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01901; adhes_NPXG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Cytolysis; Direct protein sequencing;
KW Hemolysis; Membrane; Signal; Toxin; Virulence.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:2407716"
FT CHAIN 30..1577
FT /note="Hemolysin"
FT /id="PRO_0000013355"
FT REGION 437..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:5SZ8"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6PYK"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:6PZL"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 142..165
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 188..203
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 210..221
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:6PYK"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:6PZL"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:4W8Q"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:6PYK"
SQ SEQUENCE 1577 AA; 165869 MW; 175975E0C924B2D9 CRC64;
MKSKNFKLSP SGRLAASLAI IFVSLNAYGN GIVPDAGHQG PDVSAVNGGT QVINIVTPNN
EGISHNQYQD FNVGKPGAVF NNALEAGQSQ LAGHLNANSN LNGQAASLIL NEVVSRNPSF
LLGQQEVFGI AAEYVLSNPN GITCDGCGFI NTSRSSLVVG NPLFENGQLK GYSTLNNTNL
LSLGKNGLNT TGLLDLIAPR IDSRGKITAA EISAFTGQNT FSQHFDILSS QKPVSALDSY
FFGSMQSGRI RIINTAEGSG VKLAGKFTAD NDLSVKADNI QTDSQVRYDS YDKDGSENYQ
NYRGGITVNN SGSSQTLTKT ELKGKNITLV ASSHNQIKAS DLMGDDITLQ GADLTIDGKQ
LQQKETDIDN RWFYSWKYDV TKEKEQIQQI GSQIDAKNNA TLTATKGDVT LDAAKINAGN
NLAINANKDI HINGLVEKES RSENGNKRNH TSRLESGSWS NSHQTETLKA SELTAGKDLG
LDAQGSITAQ GAKLHANENV LVNAKDNINL NVQKTNNDKT VTDNHVMWGG IGGGQNKNNN
NQQQVSHATQ LTADGQLLLA ADNNVNITGS QVKGNQGAFV KTTQGDVVID NALSETISKI
DERTGTAFNI TKSSHKNETN KQTSTGSELI SDAQLTVVSG NDVNVIGSLI KSADKLGIHS
LGDINVKSAQ QVTKIDDEKT SLAITGHAKE VEDKQYSAGF HITHTTNKNT STETEQANST
ISGANVDLQA NKDVTFAGSD LKTTAGNASI TGDNVAFVST ENKKQTDNTD TTISGGFSYT
GGVDKVGSKA DFQYDKQHTQ TEVTKNRGSQ TEVAGDLTIT ANKDLLHEGA SHHVEGRYQE
SGENIQHLAV NDSETSKTDS LNVGIDVGVN LDYSGVTKPV KKAIEDGVNT TKPGNNTDLT
KKVTARDAIA NLANLSNLET PNVGVEVGIK GGGSQQSQTD SQAVSTSINA GKIDIDSNNK
LHDQGTHYQS TQEGISLTAN THTSEATLDK HQTTFHETKG GGQIGVSTKT GSDITVAIKG
EGQTTDNALM ETKAKGSQFT SNGDISINVG ENAHYEGAQF DAQKGKTVIN AGGDLTLAQA
TDTHSESQSN VNGSANLKVG TTPESKDYGG GFNAGTTHHS KEQTTAKVGT ITGSQGIELN
AGHNLTLQGT HLSSEQDIAL NATNKVDLQS ASSEHTEKGN NLSGGVQAGF GKKMTDDASS
VNGLGSAQFA IGKQDEKSVS REGGTINNSG NLTINGNSVH LQGAQVNSKD TQLTSQSGDI
EITSAQSTDY KNNWGTDIGF NGKKTNNTPK EVTEEKPATS IHNIGGKLLV NVEDQQKTSH
QNATLETGTL TINSNKDLTL SGANVTADSV TGNVGGSLNI ASQKESDRHV TVGVNVGYNH
TNDPKSSQVN KTAKAGGSLL EKTIKDTIDS GIKSSTDAIS DKYNSLSSTI ADKTGISDET
KAKIDQGFGK VGNGIKNIVT GAEGHTANAD IKVTHVDNDA VTKTTSLTSN NDLSLNVNGS
TKLTGAEIVS QQGQVDLGGS SVKLENIEGH HYEAGADLDL KSSVVDLAKQ LVGGDISFKS
PVKTNETVNT KASISEK
