ID   HLYA_SERMA              Reviewed;        1608 AA.
AC   P15320;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Hemolysin;
DE   Flags: Precursor;
GN   Name=shlA;
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 31-40.
RC   STRAIN=SN8;
RX   PubMed=3290200; DOI=10.1128/jb.170.7.3177-3188.1988;
RA   Poole K., Schiebel E., Braun V.;
RT   "Molecular characterization of the hemolysin determinant of Serratia
RT   marcescens.";
RL   J. Bacteriol. 170:3177-3188(1988).
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. ShlA
CC       requires ShlB function.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane.
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DR   EMBL; M22618; AAA50323.1; -; Genomic_DNA.
DR   PIR; A28182; A28182.
DR   AlphaFoldDB; P15320; -.
DR   SMR; P15320; -.
DR   STRING; 273526.SMDB11_3737; -.
DR   TCDB; 1.C.75.1.1; the bacterial-type pore-forming toxin (b-pft) family.
DR   PRIDE; P15320; -.
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; 7.
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   Cell outer membrane; Cytolysis; Direct protein sequencing; Hemolysis;
KW   Membrane; Signal; Toxin; Virulence.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000269|PubMed:3290200"
FT   CHAIN           31..1608
FT                   /note="Hemolysin"
FT                   /id="PRO_0000013356"
FT   REGION          296..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          716..737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          971..1030
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1168..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1437..1469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        982..996
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        998..1030
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1168..1197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1608 AA;  165079 MW;  D669B476FE7DAD51 CRC64;
     MKNNNFRLSA AGKLAAALAI ILAASAGAYA AEIVAANGAN GPGVSTAATG AQVVDIVAPN
     GNGLSHNQYQ DFNVNQPGAV LNNSREAGLS QLAGQLGANP NLGGREASVI LNEVIGRNPS
     LLHGQQEIFG MAADYVLANP NGISCQSCGF INTSHSSLVV GNPLVENGVL QGYSTFGNRN
     TLSLNGTLNA GGVLDLIAPK IDSRGEVIVQ DFKQSNGKVT SAAINAISGL NRVARDGTVQ
     ASQQMPTALD SYYLGSMQAG RINIINTAQG SGVKLAGSLN AGDELKVKAY DIRSESRVDD
     ASSNKNGGDN YQNYRGGIYV NDRSSSQTLT RTELKGKNIS LVADNHAHLT ATDIRGEDIT
     LQGGKLTLDG QQLKQTQGHT DDRWFYSWQY DVTREREQLQ QAGSTVAASG SAKLISTQED
     VKLLGANVSA DRALSVKAAR DVHLAGLVEK DKSSERGYQR NHTSSLRTGR WSNSDESESL
     KASELRSEGE LTLKAGRNVS TQGAKVHAQR DLTIDADNQI QVGVQKTANA KAVRDDKTSW
     GGIGGGDNKN NSNRREISHA SELTSGGTLR LNGQQGVTIT GSKARGQKGG EVTATHGGLR
     IDNALSTTVD KIDARTGTAF NITSSSHKAD NSYQSSTASE LKSDTNLTLV SHKDADVIGS
     QVASGGELSV ESKTGNINVK AAERQQNIDE QKTALTVNGY AKEAGDKQYR AGLRIEHTRD
     SEKTTRTENS ASSLSGGSVK LKAEKDVTFS GSKLVADKGD ASVSGNKVSF LAADDKTASN
     TEQTKIGGGF YYTGGIDKLG SGVEAGYENN KTQAQSSKAI TSGSDVKGNL TINARDKLTQ
     QGAQHSVGGA YQENAAGVDH LAAADTASTT TTKTDVGVNI GANVDYSAVT RPVERAVGKA
     AKLDATGVIN DIGGIGAPNV GLDIGAQGGS SEKRSSSSQA VVSSVQAGSI DINAKGEVRD
     QGTQYQASKG AVNLTADSHR SEAAANRQDE QSRDTRGSAG VRVYTTTGSD LTVDAKGEGG
     TQRSNSSASQ AVTGSIDAAN GINVNVKKDA IYQGTALNGG RGKTAVNAGG DIRLDQASDK
     QSESRSGFNV KASAKGGFTA DSKNFGAGFG GGTHNGESSS STAQVGNISG QQGVELKAGR
     DLTLQGTDVK SQGDVSLSAG NKVALQAAES TQTRKESKLS GNIDLGAGSS DSKEKTGGNL
     SAGGAFDIAK VNESATERQG ATIASDGKVT LSANGKGDDA LHLQGAKVSG GSAALEAKNG
     GILLESAKNE QHKDNWSLGI KANAKGGQTF NKDAGGKVDP NTGKDTHTLG AGLKVGVEQQ
     DKTTHANTGI TAGDVTLNSG KDTRLAGARV DADSVQGKVG GDLHVESRKD VENGVKVDVD
     AGLSHSNDPG SSITSKLSKV GTPRYAGKVK EKLEAGVNKV ADATTDKYNS VARRLDPQQD
     TTGAVSFSKA EGKVTLPATP AGEKPQGPLW DRGARTVGGA VKDSITGPAG RQGHLKVNAD
     VVNNNAVGEQ SAIAGKNGVA LQVGGQTQLT GGEIRSQQGK VELGGSQVSQ QDVNGQRYQG
     GGRVDAAATV GGLLGGAAKQ SVAGNVPFAS GHASTQQADA KAGVFSGK