DESS_MYXXA
ID DESS_MYXXA Reviewed; 173 AA.
AC P02966;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Development-specific protein S;
DE AltName: Full=Spore coat protein S;
GN Name=tps;
OS Myxococcus xanthus.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=34;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6316328; DOI=10.1073/pnas.80.22.6829;
RA Inouye S., Franceschini T., Inouye M.;
RT "Structural similarities between the development-specific protein S from a
RT Gram-negative bacterium, Myxococcus xanthus, and calmodulin.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:6829-6833(1983).
RN [2]
RP CALCIUM-BINDING SITES, AND MUTAGENESIS.
RX PubMed=3121626; DOI=10.1016/s0021-9258(19)57286-6;
RA Teintze M., Inouye M., Inouye S.;
RT "Characterization of calcium-binding sites in development-specific protein
RT S of Myxococcus xanthus using site-specific mutagenesis.";
RL J. Biol. Chem. 263:1199-1203(1988).
RN [3]
RP SIMILARITY TO BETA/GAMMA-CRYSTALLIN FAMILY.
RX PubMed=3925350; DOI=10.1038/315771a0;
RA Wistow G., Summers L., Blundell T.;
RT "Myxococcus xanthus spore coat protein S may have a similar structure to
RT vertebrate lens beta gamma-crystallins.";
RL Nature 315:771-773(1985).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=8183906; DOI=10.1073/pnas.91.10.4308;
RA Bagby S., Harvey T.S., Eagle S.G., Inouye S., Ikura M.;
RT "Structural similarity of a developmentally regulated bacterial spore coat
RT protein to beta gamma-crystallins of the vertebrate eye lens.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4308-4312(1994).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=8081742; DOI=10.1016/s0969-2126(00)00013-7;
RA Bagby S., Harvey T.S., Eagle S.G., Inouye S., Ikura M.;
RT "NMR-derived three-dimensional solution structure of protein S complexed
RT with calcium.";
RL Structure 2:107-122(1994).
RN [6] {ECO:0007744|PDB:1NPS}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-89 IN COMPLEX WITH CALCIUM.
RX PubMed=10064714; DOI=10.1006/jmbi.1999.2582;
RA Wenk M., Baumgartner R., Holak T.A., Huber R., Jaenicke R., Mayr E.M.;
RT "The domains of protein S from Myxococcus xanthus: structure, stability and
RT interactions.";
RL J. Mol. Biol. 286:1533-1545(1999).
CC -!- FUNCTION: Protein S, induced in large amounts during fruiting body
CC formation, assembles on the surface of myxospores in the presence of
CC calcium ions.
CC -!- DOMAIN: Has a two-domain beta-structure, folded into four very similar
CC Greek key motifs. The N-terminal domain (NPS) binds 2 calcium ions.
CC {ECO:0000269|PubMed:10064714}.
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR EMBL; J01745; AAA25407.1; -; Genomic_DNA.
DR PIR; A03490; DZYZSX.
DR RefSeq; WP_020477824.1; NZ_JABFNQ010000113.1.
DR PDB; 1NPS; X-ray; 1.80 A; A=2-89.
DR PDB; 1PRR; NMR; -; A=1-173.
DR PDB; 1PRS; NMR; -; A=1-173.
DR PDBsum; 1NPS; -.
DR PDBsum; 1PRR; -.
DR PDBsum; 1PRS; -.
DR AlphaFoldDB; P02966; -.
DR SMR; P02966; -.
DR GeneID; 41362691; -.
DR EvolutionaryTrace; P02966; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR001064; Beta/gamma_crystallin.
DR InterPro; IPR011024; G_crystallin-like.
DR Pfam; PF00030; Crystall; 1.
DR SMART; SM00247; XTALbg; 2.
DR SUPFAM; SSF49695; SSF49695; 2.
DR PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Metal-binding; Repeat; Sporulation.
FT CHAIN 1..173
FT /note="Development-specific protein S"
FT /id="PRO_0000057606"
FT DOMAIN 2..46
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 48..86
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 91..135
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 136..173
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 87..90
FT /note="Connecting peptide"
FT BINDING 8
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10064714,
FT ECO:0007744|PDB:1NPS"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10064714,
FT ECO:0007744|PDB:1NPS"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10064714,
FT ECO:0007744|PDB:1NPS"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10064714,
FT ECO:0007744|PDB:1NPS"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10064714,
FT ECO:0007744|PDB:1NPS"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10064714,
FT ECO:0007744|PDB:1NPS"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10064714,
FT ECO:0007744|PDB:1NPS"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10064714,
FT ECO:0007744|PDB:1NPS"
FT MUTAGEN 40
FT /note="S->R: Suppresses completely calcium-binding."
FT /evidence="ECO:0000269|PubMed:3121626"
FT MUTAGEN 129
FT /note="S->R: Lower calcium affinity."
FT /evidence="ECO:0000269|PubMed:3121626"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1NPS"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:1NPS"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:1NPS"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1NPS"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:1NPS"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1NPS"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1NPS"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:1NPS"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:1NPS"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1NPS"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1NPS"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1PRR"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1PRR"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1PRR"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1PRR"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:1PRS"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:1PRR"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:1PRR"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:1PRR"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:1PRR"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1PRR"
SQ SEQUENCE 173 AA; 18793 MW; C504A6409752C454 CRC64;
MANITVFYNE DFQGKQVDLP PGNYTRAQLA ALGIENNTIS SVKVPPGVKA ILYQNDGFAG
DQIEVVANAE ELGPLNNNVS SIRVISVPVQ PRARFFYKEQ FDGKEVDLPP GQYTQAELER
YGIDNNTISS VKPQGLAVVL FKNDNFSGDT LPVNSDAPTL GAMNNNTSSI RIS
