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Database: UniProt
Entry: Q8E0S9_STRA5
LinkDB: Q8E0S9_STRA5
Original site: Q8E0S9_STRA5 
ID   Q8E0S9_STRA5            Unreviewed;       554 AA.
AC   Q8E0S9;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   18-JUN-2025, entry version 125.
DE   SubName: Full=Cell wall surface anchor family protein {ECO:0000313|EMBL:AAM99537.1};
GN   OrderedLocusNames=SAG0645 {ECO:0000313|EMBL:AAM99537.1};
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435 {ECO:0000313|EMBL:AAM99537.1, ECO:0000313|Proteomes:UP000000821};
RN   [1] {ECO:0000313|EMBL:AAM99537.1, ECO:0000313|Proteomes:UP000000821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R {ECO:0000313|Proteomes:UP000000821};
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin S., Kolonay J.F., Umayam L.A., Madupu R., Lewis M.R.,
RA   Radune D., Fedorova N.B., Scanlan D., Khouri H., Mulligan S., Carty H.A.,
RA   Cline R.T., Gill J., Scarselli M., Mora M., Iacobini E.T., Brettoni C.,
RA   Galli G., Mariani M., Vegni F., Maione D., Rinaudo D., Rappuoli R.,
RA   Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
RN   [2] {ECO:0007829|PDB:3PF2, ECO:0007829|PDB:3PG2}
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 200-518 IN COMPLEX WITH CA(2+).
RX   PubMed=21333654; DOI=10.1016/j.jmb.2011.02.024;
RA   Vengadesan K., Ma X., Dwivedi P., Ton-That H., Narayana S.V.;
RT   "A model for group B Streptococcus pilus type 1: the structure of a 35-kDa
RT   C-terminal fragment of the major pilin GBS80.";
RL   J. Mol. Biol. 407:731-743(2011).
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DR   EMBL; AE009948; AAM99537.1; -; Genomic_DNA.
DR   RefSeq; NP_687665.1; NC_004116.1.
DR   RefSeq; WP_000777402.1; NC_004116.1.
DR   PDB; 3PF2; X-ray; 1.70 A; A=200-518.
DR   PDB; 3PG2; X-ray; 1.80 A; A/B=200-518.
DR   PDBsum; 3PF2; -.
DR   PDBsum; 3PG2; -.
DR   AlphaFoldDB; Q8E0S9; -.
DR   SMR; Q8E0S9; -.
DR   STRING; 208435.SAG0645; -.
DR   GeneID; 66885554; -.
DR   KEGG; sag:SAG0645; -.
DR   PATRIC; fig|208435.3.peg.647; -.
DR   HOGENOM; CLU_029024_1_1_9; -.
DR   OrthoDB; 2249722at2; -.
DR   EvolutionaryTrace; Q8E0S9; -.
DR   Proteomes; UP000000821; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.740; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR026466; Fim_isopep_form_D2_dom.
DR   InterPro; IPR048052; FM1-like.
DR   InterPro; IPR032334; GramPos_pilinBB.
DR   InterPro; IPR032364; GramPos_pilinD1_N.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR041033; SpaA_PFL_dom_1.
DR   NCBIfam; NF033902; iso_D2_wall_anc; 1.
DR   NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR   NCBIfam; TIGR04226; RrgB_K2N_iso_D2; 1.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF16569; GramPos_pilinBB; 1.
DR   Pfam; PF16555; GramPos_pilinD1; 1.
DR   Pfam; PF17802; SpaA; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3PF2, ECO:0007829|PDB:3PG2};
KW   Calcium {ECO:0007829|PDB:3PF2, ECO:0007829|PDB:3PG2};
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0007829|PDB:3PF2, ECO:0007829|PDB:3PG2};
KW   Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000821};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..554
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038497120"
FT   TRANSMEM        525..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          46..201
FT                   /note="Gram-positive pilin subunit D1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16555"
FT   DOMAIN          224..361
FT                   /note="Gram-positive pilin backbone subunit 2 Cna-B-like"
FT                   /evidence="ECO:0000259|Pfam:PF16569"
FT   DOMAIN          385..495
FT                   /note="SpaA-like prealbumin fold"
FT                   /evidence="ECO:0000259|Pfam:PF17802"
FT   DOMAIN          514..550
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|Pfam:PF00746"
FT   REGION          358..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         209
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3PF2, ECO:0007829|PDB:3PG2"
FT   BINDING         210
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3PF2, ECO:0007829|PDB:3PG2"
FT   BINDING         211
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3PF2, ECO:0007829|PDB:3PG2"
FT   BINDING         218
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3PF2, ECO:0007829|PDB:3PG2"
FT   BINDING         244
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3PF2, ECO:0007829|PDB:3PG2"
FT   BINDING         358
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3PF2, ECO:0007829|PDB:3PG2"
FT   BINDING         360
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3PF2, ECO:0007829|PDB:3PG2"
FT   BINDING         362
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3PF2, ECO:0007829|PDB:3PG2"
FT   BINDING         364
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3PF2, ECO:0007829|PDB:3PG2"
FT   BINDING         366
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3PF2, ECO:0007829|PDB:3PG2"
SQ   SEQUENCE   554 AA;  60168 MW;  64498D4B49729AD1 CRC64;
     MKLSKKLLFS AAVLTMVAGS TVEPVAQFAT GMSIVRAAEV SQERPAKTTV NIYKLQADSY
     KSEITSNGGI ENKDGEVISN YAKLGDNVKG LQGVQFKRYK VKTDISVDEL KKLTTVEAAD
     AKVGTILEEG VSLPQKTNAQ GLVVDALDSK SNVRYLYVED LKNSPSNITK AYAVPFVLEL
     PVANSTGTGF LSEINIYPKN VVTDEPKTDK DVKKLGQDDA GYTIGEEFKW FLKSTIPANL
     GDYEKFEITD KFADGLTYKS VGKIKIGSKT LNRDEHYTID EPTVDNQNTL KITFKPEKFK
     EIAELLKGMT LVKNQDALDK ATANTDDAAF LEIPVASTIN EKAVLGKAIE NTFELQYDHT
     PDKADNPKPS NPPRKPEVHT GGKRFVKKDS TETQTLGGAE FDLLASDGTA VKWTDALIKA
     NTNKNYIAGE AVTGQPIKLK SHTDGTFEIK GLAYAVDANA EGTAVTYKLK ETKAPEGYVI
     PDKEIEFTVS QTSYNTKPTD ITVDSADATP DTIKNNKRPS IPNTGGIGTA IFVAIGAAVM
     AFAVKGMKRR TKDN
//
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