SSGB_THEFY
ID SSGB_THEFY Reviewed; 138 AA.
AC Q47N25;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Sporulation-specific cell division protein SsgB {ECO:0000303|PubMed:19567872};
DE AltName: Full=Sporulation of Streptomyces griseus-like protein B {ECO:0000303|PubMed:19567872};
DE AltName: Full=SsgA-like protein B {ECO:0000303|PubMed:19567872};
DE Short=SALP B {ECO:0000303|PubMed:19567872};
GN Name=ssgB {ECO:0000303|PubMed:19567872};
GN OrderedLocusNames=Tfu_2111 {ECO:0000312|EMBL:AAZ56144.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000312|EMBL:AAZ56144.1};
RN [1] {ECO:0007744|PDB:3CM1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS),
RP FUNCTION, AND SUBUNIT.
RC STRAIN=YX {ECO:0000303|PubMed:19567872};
RX PubMed=19567872; DOI=10.1074/jbc.m109.018564;
RA Xu Q., Traag B.A., Willemse J., McMullan D., Miller M.D., Elsliger M.A.,
RA Abdubek P., Astakhova T., Axelrod H.L., Bakolitsa C., Carlton D., Chen C.,
RA Chiu H.J., Chruszcz M., Clayton T., Das D., Deller M.C., Duan L.,
RA Ellrott K., Ernst D., Farr C.L., Feuerhelm J., Grant J.C., Grzechnik A.,
RA Grzechnik S.K., Han G.W., Jaroszewski L., Jin K.K., Klock H.E., Knuth M.W.,
RA Kozbial P., Krishna S.S., Kumar A., Marciano D., Minor W., Mommaas A.M.,
RA Morse A.T., Nigoghossian E., Nopakun A., Okach L., Oommachen S.,
RA Paulsen J., Puckett C., Reyes R., Rife C.L., Sefcovic N., Tien H.J.,
RA Trame C.B., van den Bedem H., Wang S., Weekes D., Hodgson K.O., Wooley J.,
RA Deacon A.M., Godzik A., Lesley S.A., Wilson I.A., van Wezel G.P.;
RT "Structural and functional characterizations of SsgB, a conserved activator
RT of developmental cell division in morphologically complex actinomycetes.";
RL J. Biol. Chem. 284:25268-25279(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
RN [3]
RP FUNCTION, AND INTERACTION WITH FTSZ AND SSGA.
RX PubMed=21205868; DOI=10.1101/gad.600211;
RA Willemse J., Borst J.W., de Waal E., Bisseling T., van Wezel G.P.;
RT "Positive control of cell division: FtsZ is recruited by SsgB during
RT sporulation of Streptomyces.";
RL Genes Dev. 25:89-99(2011).
CC -!- FUNCTION: Involved in sporulation-specific cell division
CC (PubMed:19567872). Required for early stages of sporulation. Important
CC in the process of growth cessation prior to sporulation-specific cell
CC division. Recruits cell division protein FtsZ to the future septum
CC sites and tethers the contractile ring structure (Z ring) to the
CC cytoplasmic membrane during sporulation (By similarity). Stimulates
CC polymerization and filament length of FtsZ in vitro (PubMed:21205868).
CC {ECO:0000250|UniProtKB:Q9L268, ECO:0000269|PubMed:19567872,
CC ECO:0000269|PubMed:21205868}.
CC -!- SUBUNIT: Monomer (PubMed:19567872). Interacts with SsgA. Interacts with
CC FtsZ (via N-terminus) (PubMed:21205868). {ECO:0000269|PubMed:19567872,
CC ECO:0000269|PubMed:21205868}.
CC -!- SUBCELLULAR LOCATION: Cell septum {ECO:0000250|UniProtKB:Q9L268}.
CC Note=Localizes to the divisome in sporogenic aerial hyphae in a ladder-
CC like manner. Temporospatial localization is controlled by SsgA and it
CC colocalizes with SsgA in presporulation foci. Localizes to the septum
CC sites prior to FtsZ and after that colocalizes with FtsZ at the
CC divisome throughout cell division. {ECO:0000250|UniProtKB:Q9L268}.
CC -!- SIMILARITY: Belongs to the SsgA family. {ECO:0000305}.
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DR EMBL; CP000088; AAZ56144.1; -; Genomic_DNA.
DR RefSeq; WP_011292534.1; NC_007333.1.
DR PDB; 3CM1; X-ray; 2.60 A; A/B/C=1-138.
DR PDBsum; 3CM1; -.
DR AlphaFoldDB; Q47N25; -.
DR SMR; Q47N25; -.
DR STRING; 269800.Tfu_2111; -.
DR DNASU; 3581046; -.
DR EnsemblBacteria; AAZ56144; AAZ56144; Tfu_2111.
DR KEGG; tfu:Tfu_2111; -.
DR eggNOG; ENOG5032RFA; Bacteria.
DR HOGENOM; CLU_126599_0_1_11; -.
DR OMA; NDEPVEW; -.
DR OrthoDB; 1627707at2; -.
DR EvolutionaryTrace; Q47N25; -.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:2000246; P:positive regulation of FtsZ-dependent cytokinesis; IDA:UniProtKB.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 2.30.31.20; -; 1.
DR InterPro; IPR006776; SsgB.
DR InterPro; IPR038658; SsgB_sf.
DR Pfam; PF04686; SsgA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Septation; Sporulation.
FT CHAIN 1..138
FT /note="Sporulation-specific cell division protein SsgB"
FT /id="PRO_0000435022"
FT STRAND 7..17
FT /evidence="ECO:0007829|PDB:3CM1"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:3CM1"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:3CM1"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:3CM1"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:3CM1"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:3CM1"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:3CM1"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:3CM1"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:3CM1"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:3CM1"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:3CM1"
SQ SEQUENCE 138 AA; 15251 MW; 9293B08C1D3EC6B9 CRC64;
MSSSGTSITC EVGLQLIVPD RAPVPLVARL DYSVDDPYAI RAAFHVGDDE PVEWIFAREL
LTVGIIRETG EGDVRIWPSQ DGKERMVNIA LSSPFGQARF HAQVAPLSEF LHRTYELVPA
GQESDYIDID AEIAEHLS
