ID A0YKP6_LYNSP Unreviewed; 681 AA.
AC A0YKP6;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Hemolysin-type calcium-binding toxin {ECO:0000313|EMBL:EAW38585.1};
GN ORFNames=L8106_07279 {ECO:0000313|EMBL:EAW38585.1};
OS Lyngbya sp. (strain PCC 8106) (Lyngbya aestuarii (strain CCY9616)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Lyngbya.
OX NCBI_TaxID=313612 {ECO:0000313|EMBL:EAW38585.1, ECO:0000313|Proteomes:UP000000737};
RN [1] {ECO:0000313|EMBL:EAW38585.1, ECO:0000313|Proteomes:UP000000737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC8106 {ECO:0000313|Proteomes:UP000000737};
RA Stal L., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAW38585.1}.
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DR EMBL; AAVU01000004; EAW38585.1; -; Genomic_DNA.
DR RefSeq; WP_009783052.1; NZ_AAVU01000004.1.
DR AlphaFoldDB; A0YKP6; -.
DR eggNOG; COG2931; Bacteria.
DR Proteomes; UP000000737; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 2.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR Pfam; PF00353; HemolysinCabind; 4.
DR PRINTS; PR00313; CABNDNGRPT.
DR SUPFAM; SSF51120; beta-Roll; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT REGION 1..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..165
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..272
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..372
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 73117 MW; 2A828C39F9636AB5 CRC64;
MEPETRLELQ PESSEEDTSL PESQTSESPE LEDEEDSPLL DPQPEIAESG ESDSASNAED
LSESEPRSPV ESSEDESKET PASSDPQIIQ PESKSGSNSD VDVPPESNTE PETRTEVEPE
SPDENTPPPQ SQTPQSPNLE DEQDSPLNPQ PEIDETEEDS PPQAEVEPPE SEPRSPVESS
EDESKETPAS SDPQIIQPES KSGSNSNVEI PPESNTEPET RTEVEPESPD ENTPPPQSQT
PQSPNLEDEQ DSPLNPQPEI DETEEDSPPQ AEVEPPESEP RTPVEPSEDE PKETPTTTDP
QTTPEPESKS GSDSNVDVPP QSNTEPETRP EVEPEPPDDT TPDNPQPTQP DSQPDSQPED
PDVDPPSTPD NIPVVGTPSM DDFPPTTEEE SLPEPVLTPE PEFEPTPPDI SGFTVLTISG
TDSSDNLLGS DNDSEIFRGF SGDDIIFGFA QPDNFFGGEG NDLMFGNQNE DFLEGNDGND
TVFGGKENDT LLGNAGEDSL FGDQDDDLLY GGENADWLNG NLGNDTIKGG DGDDLAYGGQ
GNDVLEGEAG NDLVSGDNGD DVLIGADPNI TDAGQNEIDT LVGGVGADTF VLGDEIQVYY
DDGDLNSSGL EDYALIQDFD NTQDIIQLAG NAEDYRLDVQ PEGLPQGTAL YHTVGGQDEL
IAIIQGTSFP VVLEEDYFTF V
//
