ID   SLAP_SYNY3              Reviewed;        1741 AA.
AC   P73817;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=S-layer protein {ECO:0000303|PubMed:24078613};
DE   AltName: Full=Hemolysin-like protein {ECO:0000303|PubMed:16672608};
DE            Short=HLP {ECO:0000303|PubMed:16672608};
GN   OrderedLocusNames=sll1951 {ECO:0000312|EMBL:BAA17871.1};
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND GLYCOSYLATION.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=16672608; DOI=10.1128/jb.188.10.3535-3542.2006;
RA   Sakiyama T., Ueno H., Homma H., Numata O., Kuwabara T.;
RT   "Purification and characterization of a hemolysin-like protein, Sll1951, a
RT   nontoxic member of the RTX protein family from the Cyanobacterium
RT   Synechocystis sp. strain PCC 6803.";
RL   J. Bacteriol. 188:3535-3542(2006).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, DISRUPTION PHENOTYPE, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=24078613; DOI=10.1128/jb.00615-13;
RA   Trautner C., Vermaas W.F.;
RT   "The sll1951 gene encodes the surface layer protein of Synechocystis sp.
RT   strain PCC 6803.";
RL   J. Bacteriol. 195:5370-5380(2013).
CC   -!- FUNCTION: S-layer protein. The S-layer is a paracrystalline mono-
CC       layered assembly of proteins which coats the surface of bacteria
CC       (PubMed:24078613). Under laboratory conditions, has a supportive but
CC       not a critical role in the function of the cyanobacterium
CC       (PubMed:24078613). Shows no apparent hemolytic activity against sheep
CC       erythrocytes, however, a slight hemolytic activity is detected during
CC       the conformational change caused by the rebinding of Ca(2+)
CC       (PubMed:16672608). {ECO:0000269|PubMed:16672608,
CC       ECO:0000269|PubMed:24078613}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer
CC       {ECO:0000269|PubMed:16672608, ECO:0000269|PubMed:24078613}.
CC   -!- DOMAIN: Contains GGXGXDXUX nonapeptide motifs, which are found in
CC       members of the repeat in toxin (RTX) protein family, and which are
CC       implicated in Ca(2+) binding. Binds Ca(2+) and shows Ca(2+)-induced
CC       reversible conformational changes. {ECO:0000269|PubMed:16672608}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:16672608,
CC       ECO:0000269|PubMed:24078613}.
CC   -!- DISRUPTION PHENOTYPE: The deletion mutant has similar pigmentation, but
CC       a more flat, spread morphology and a shiny surface. It displays a
CC       smooth lipopolysaccharide surface as its most peripheral layer.
CC       Viability of the mutant is reduced upon exposure to lysozyme treatment
CC       and hypo-osmotic stress. {ECO:0000269|PubMed:24078613}.
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DR   EMBL; BA000022; BAA17871.1; -; Genomic_DNA.
DR   PIR; S74910; S74910.
DR   AlphaFoldDB; P73817; -.
DR   SMR; P73817; -.
DR   IntAct; P73817; 2.
DR   STRING; 1148.1652953; -.
DR   PaxDb; P73817; -.
DR   EnsemblBacteria; BAA17871; BAA17871; BAA17871.
DR   KEGG; syn:sll1951; -.
DR   eggNOG; COG2931; Bacteria.
DR   InParanoid; P73817; -.
DR   OMA; NGANEIW; -.
DR   PhylomeDB; P73817; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0030115; C:S-layer; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   Gene3D; 2.150.10.10; -; 3.
DR   InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR   InterPro; IPR001343; Hemolysn_Ca-bd.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   Pfam; PF00353; HemolysinCabind; 7.
DR   SUPFAM; SSF51120; SSF51120; 2.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 2.
PE   1: Evidence at protein level;
KW   Cell wall; Glycoprotein; Reference proteome; S-layer; Secreted.
FT   CHAIN           1..1741
FT                   /note="S-layer protein"
FT                   /id="PRO_0000444329"
FT   REGION          894..913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1741 AA;  178261 MW;  189C5A339105B9EF CRC64;
     MALSPNVIAA LQIMYTGRGV SASDLNWWAT DGANITYAEA VALFASSPDA AIKYPFFQAP
     QTADKRQYVA QVFANLYNID INDTSLVPTE ELDYWINWLS LSPDNYLDFP NALNNASAAA
     GLTDRLEALT NKADVSLSYT EALSTAGVNT FTEAQYAEAA GIIATVDDTN ASVLAAEAQI
     VEIAASLSVF TIAQAQATPN LPPAYTISDT ADNLIAGADD PVVTGANNVI ANQSPAAPLS
     VEDANILLAT ADELAAGVTW DILDTAADVL AGGAAVSGAA SVGITDIVDV ATASQLLALG
     NFDGVYAIAD TSANIVADPG VSGGATAITL SDPDVPVSVA SATFLQGLGI PVGPSYIVED
     TSANILAALS TPAIVNAAEV IVNNTDVPLS VAQAEDLLSL PNLNAGFTYI IADTLDNLSA
     APSTLLDGAV SYSLTNTNPD LGVITEAEAV IVNGATNASD FNFLVADVIL TPQADIRSGN
     SFLSVAVVEG GSIFNTLNSN DRLTGTGEDP TLSLTWQEAT FGNINTIFPV LDGIETLVAT
     LIENDLTLVS NDFDVVGQGF ITGLKNVAAS GTKGGDLELI NLQTALETVS VTNYFFGDDV
     SFSIADPELA GDNDLLLLTV DQVTEDGPDV TSIKISDFSG NGGYETLGLT SGVTTSSKGN
     TNTVDIEGIV AVESIGITGI ENLTLSTSLI GSVVKVDATG SALIPEFEGR EVFTGDLKAF
     FDDRPGGDIT FLSGSGNDEI SIARDAFTLS EDLKDVISKG HILDGGAGND ELTITGDAFS
     DTDAGHTVIG GEGNDSILLT GVAEGPIAGH VVNSFDLINE VGGAGDDDIN ISGDAIGDSA
     GHVVFGGAGE DDIFIGFDKT LAVSGNGAAL GVDLAGHVVF AGDDDDTVRI TGDSFTSDSA
     NGSGHSVEGG TGDDLIEISG DALTADPDSE TIANPFFDDS EPSDLDLFIA ADQPIPTTEE
     QYQVLLAQLG LPADYNPRNF IRGVAAISGA HTVRGGEGND VILFGPIAGE PGNGDGQHLA
     FGDEGDDFIE MTGIGSVEFN GGAGDDTLVG GDGDPILGFG NDILNGDEGN DFLFGGKGND
     NLQGGEGDDI MSGGEGDDFF FVDAGFDVIE DLGDANSETG DQFQVSEDAE AEIRVVQDWE
     ATGLTFNLGI ATLTIENPGG GSVDLSASNV PPNTNGYTVI GNIGDDEIIG SRDDDSIFGG
     RGEDSIAGLG GDDIIEGNDD DDFISGDSLL LPLLPLEEIL PFGNDDIDAG SGNDVIAGDL
     LVVTGDDIDL NLFNGGKDTI EAGLGSDITV GDWSIGAFGD IDLNASLERT AIGGDDTITT
     KQGDNGIVFP IGQVAIDNFL VGDLAAAVDG VGNDIFLTET LTVIGGDDTM TGADGLDVIV
     GDVGLFGFEF NDSEINLTNF KLGQVNGSTV SAGDDSITGE GGNDILVGDL FVGVINNNGI
     IIDGGKGFQL GKDGTTSFIG GDDSISGGDG NDFLAGDFVL VDQLSAPFDP LDPNDWTFVN
     PYATLQGQAG DSKAQAAQAA INLAQLRLEF RAVGGDDELV GGRGNDTFYG GLGADTIDIG
     NDVTVGGVGV NGANEIWYMN GAFENAAVNG ANVDNITGFN VNNDKFVFAA GANNFLSGDA
     TSGLAVQRVL NLQAGNTVFN LNDPILNASA NNINDVFLAV NADNSVGASL SFSLLPGLPS
     LVEMQQINVS SGALAGREFL FINNGVAAVS SQDDFLVELT GISGTFGLDL TPNFEVREFY
     A