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Protein

Hemolysin, chromosomal

Gene

hlyA

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture by mechanisms not clearly defined.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Toxin

Keywords - Biological processi

Cytolysis, Hemolysis

Keywords - Ligandi

Calcium

Protein family/group databases

TCDBi1.C.11.1.3. the pore-forming rtx toxin (rtx-toxin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Hemolysin, chromosomal
Gene namesi
Name:hlyA
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei237 – 25923HelicalSequence analysisAdd
BLAST
Transmembranei267 – 32660HelicalSequence analysisAdd
BLAST
Transmembranei364 – 41047HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10231023Hemolysin, chromosomalPRO_0000196215Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi563 – 5631N6-palmitoyl lysine1 Publication
Lipidationi689 – 6891N6-palmitoyl lysine1 Publication

Post-translational modificationi

Palmitoylated by HlyC. The toxin only becomes active when modified.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PRIDEiP09983.

Interactioni

Protein-protein interaction databases

DIPiDIP-16932N.
STRINGi199310.c3570.

Structurei

3D structure databases

DisProtiDP00389.
ProteinModelPortaliP09983.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati731 – 74818Hemolysin-type calcium-binding 1Add
BLAST
Repeati749 – 76618Hemolysin-type calcium-binding 2Add
BLAST
Repeati767 – 78418Hemolysin-type calcium-binding 3Add
BLAST
Repeati785 – 80218Hemolysin-type calcium-binding 4Add
BLAST
Repeati815 – 83218Hemolysin-type calcium-binding 5Add
BLAST
Repeati833 – 85018Hemolysin-type calcium-binding 6Add
BLAST

Domaini

The Gly-rich region is probably involved in binding calcium, which is required for target cell-binding or cytolytic activity.
The three transmembrane domains are believed to be involved in pore formation by the cytotoxin.

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4107V48. Bacteria.
ENOG410Z1F3. LUCA.

Family and domain databases

Gene3Di2.150.10.10. 1 hit.
InterProiIPR018511. Hemolysin-typ_Ca-bd_CS.
IPR001343. Hemolysn_Ca-bd.
IPR013550. RTX_C.
IPR018504. RTX_N.
IPR003995. RTX_toxin_determinant-A.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
PfamiPF00353. HemolysinCabind. 6 hits.
PF02382. RTX. 1 hit.
PF08339. RTX_C. 1 hit.
[Graphical view]
PRINTSiPR01488. RTXTOXINA.
SUPFAMiSSF51120. SSF51120. 3 hits.
PROSITEiPS00330. HEMOLYSIN_CALCIUM. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09983-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTITAAQIK STLQSAKQSA ANKLHSAGQS TKDALKKAAE QTRNAGNRLI
60 70 80 90 100
LLIPKDYKGQ GSSLNDLVRT ADELGIEVQY DEKNGTAITK QVFGTAEKLI
110 120 130 140 150
GLTERGVTIF APQLDKLLQK YQKAGNKLGG SAENIGDNLG KAGSVLSTFQ
160 170 180 190 200
NFLGTALSSM KIDELIKKQK SGGNVSSSEL AKASIELINQ LVDTAASLNN
210 220 230 240 250
VNSFSQQLNK LGSVLSNTKH LNGVGNKLQN LPNLDNIGAG LDTVSGILSA
260 270 280 290 300
ISASFILSNA DADTGTKAAA GVELTTKVLG NVGKGISQYI IAQRAAQGLS
310 320 330 340 350
TSAAAAGLIA SVVTLAISPL SFLSIADKFK RANKIEEYSQ RFKKLGYDGD
360 370 380 390 400
SLLAAFHKET GAIDASLTRI STVLASVSSG ISAAATTSLV GAPVSALVGA
410 420 430 440 450
VTGIISGILE ASKQAMFEHV ASKMADVIAE WEKKHGKNYF ENGYDARHAA
460 470 480 490 500
FLEDNFKILS QYNKEYSVER SVLITQQHWD TLIGELAGVT RNGDKTLSGK
510 520 530 540 550
SYIDYYEEGK RLEKKPDEFQ KQVFDPLKGN IDLSDSKSST LLKFVTPLLT
560 570 580 590 600
PGEEIRERRQ SGKYEYITEL LVKGVDKWTV KGVQDKGSVY DYSNLIQHAS
610 620 630 640 650
VGNNQYREIR IESHLGDGDD KVFLSAGSAN IYAGKGHDVV YYDKTDTGYL
660 670 680 690 700
TIDGTKATEA GNYTVTRVLG GDVKVLQEVV KEQEVSVGKR TEKTQYRSYE
710 720 730 740 750
FTHINGKNLT ETDNLYSVEE LIGTTRADKF FGSKFADIFH GADGDDHIEG
760 770 780 790 800
NDGNDRLYGD KGNDTLSGGN GDDQLYGGDG NDKLIGGAGN NYLNGGDGDD
810 820 830 840 850
ELQVQGNSLA KNVLSGGKGN DKLYGSEGAD LLDGGEGNDL LKGGYGNDIY
860 870 880 890 900
RYLSGYGHHI IDDDGGKDDK LSLADIDFRD VAFRREGNDL IMYKAEGNVL
910 920 930 940 950
SIGHKNGITF KNWFEKESGD ISNHQIEQIF DKDGRVITPD SLKKALEYQQ
960 970 980 990 1000
SNNKASYVYG NDALAYGSQG NLNPLINEIS KIISAAGNFD VKEERAAASL
1010 1020
LQLSGNASDF SYGRNSITLT ASA
Length:1,023
Mass (Da):109,867
Last modified:July 1, 1989 - v1
Checksum:i196D5C0A9A28B54D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61A → T in strain: 2001.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10133 Genomic DNA. Translation: AAA23975.1.
X02768 Genomic DNA. Translation: CAA26546.1.
PIRiA24433. LEECA.
S10056.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10133 Genomic DNA. Translation: AAA23975.1.
X02768 Genomic DNA. Translation: CAA26546.1.
PIRiA24433. LEECA.
S10056.

3D structure databases

DisProtiDP00389.
ProteinModelPortaliP09983.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-16932N.
STRINGi199310.c3570.

Protein family/group databases

TCDBi1.C.11.1.3. the pore-forming rtx toxin (rtx-toxin) family.

Proteomic databases

PRIDEiP09983.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107V48. Bacteria.
ENOG410Z1F3. LUCA.

Family and domain databases

Gene3Di2.150.10.10. 1 hit.
InterProiIPR018511. Hemolysin-typ_Ca-bd_CS.
IPR001343. Hemolysn_Ca-bd.
IPR013550. RTX_C.
IPR018504. RTX_N.
IPR003995. RTX_toxin_determinant-A.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
PfamiPF00353. HemolysinCabind. 6 hits.
PF02382. RTX. 1 hit.
PF08339. RTX_C. 1 hit.
[Graphical view]
PRINTSiPR01488. RTXTOXINA.
SUPFAMiSSF51120. SSF51120. 3 hits.
PROSITEiPS00330. HEMOLYSIN_CALCIUM. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHLYAC_ECOLX
AccessioniPrimary (citable) accession number: P09983
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 11, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The hemolysin of E.coli is produced predominantly by strains causing extraintestinal infections, such as those of the urinary tract.

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.