CDVB_SULAC
ID CDVB_SULAC Reviewed; 261 AA.
AC Q4J924;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Cell division protein B {ECO:0000305};
DE AltName: Full=ESCRT-III homolog {ECO:0000305};
GN Name=cdvB {ECO:0000303|PubMed:18987308};
GN OrderedLocusNames=Saci_1373 {ECO:0000312|EMBL:AAY80707.1};
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=18987308; DOI=10.1073/pnas.0809467105;
RA Lindaas A.C., Karlsson E.A., Lindgren M.T., Ettema T.J., Bernander R.;
RT "A unique cell division machinery in the Archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18942-18946(2008).
RN [3]
RP FUNCTION, INTERACTION WITH CDVA, AND DOMAIN.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=21255729; DOI=10.1016/j.molcel.2010.12.018;
RA Samson R.Y., Obita T., Hodgson B., Shaw M.K., Chong P.L., Williams R.L.,
RA Bell S.D.;
RT "Molecular and structural basis of ESCRT-III recruitment to membranes
RT during archaeal cell division.";
RL Mol. Cell 41:186-196(2011).
RN [4] {ECO:0007744|PDB:2W2U}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 182-195, FUNCTION, SUBCELLULAR
RP LOCATION, INDUCTION, AND INTERACTION WITH CDVC.
RX PubMed=19008417; DOI=10.1126/science.1165322;
RA Samson R.Y., Obita T., Freund S.M., Williams R.L., Bell S.D.;
RT "A role for the ESCRT system in cell division in archaea.";
RL Science 322:1710-1713(2008).
CC -!- FUNCTION: Part of a cell division machinery (PubMed:18987308,
CC PubMed:19008417, PubMed:21255729). The CdvA, CdvB and CdvC proteins
CC polymerize between segregating nucleoids and persist throughout cell
CC division, forming a successively smaller structure during constriction
CC (PubMed:18987308). {ECO:0000269|PubMed:18987308,
CC ECO:0000269|PubMed:19008417, ECO:0000269|PubMed:21255729}.
CC -!- SUBUNIT: Interacts with CdvA (PubMed:21255729). Interacts with CdvC
CC (PubMed:19008417). {ECO:0000269|PubMed:19008417,
CC ECO:0000269|PubMed:21255729}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:18987308,
CC ECO:0000269|PubMed:19008417}. Note=Forms, with CdvA, colocalized band-
CC like structures between segregating nucleoids (PubMed:18987308).
CC Localizes to the mid-cell in dividing cells (PubMed:19008417).
CC {ECO:0000269|PubMed:18987308, ECO:0000269|PubMed:19008417}.
CC -!- INDUCTION: Induced around the genome segregation and cell division
CC stages (PubMed:18987308). Down-regulated after UV irradiation,
CC indicating division inhibition in response to DNA damage
CC (PubMed:18987308). Expression is highest in dividing cells
CC (PubMed:19008417). {ECO:0000269|PubMed:18987308,
CC ECO:0000269|PubMed:19008417}.
CC -!- DOMAIN: The winged-helix-like (wH-like) C-terminal extension is
CC necessary and sufficient for interaction with CdvA.
CC {ECO:0000269|PubMed:21255729}.
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DR EMBL; CP000077; AAY80707.1; -; Genomic_DNA.
DR RefSeq; WP_011278209.1; NC_007181.1.
DR PDB; 2W2U; X-ray; 2.20 A; C/D=182-195.
DR PDBsum; 2W2U; -.
DR AlphaFoldDB; Q4J924; -.
DR SMR; Q4J924; -.
DR STRING; 330779.Saci_1373; -.
DR TCDB; 3.A.31.1.3; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR EnsemblBacteria; AAY80707; AAY80707; Saci_1373.
DR GeneID; 3472938; -.
DR KEGG; sai:Saci_1373; -.
DR PATRIC; fig|330779.12.peg.1325; -.
DR eggNOG; arCOG00453; Archaea.
DR HOGENOM; CLU_1072074_0_0_2; -.
DR OMA; RKMIKII; -.
DR EvolutionaryTrace; Q4J924; -.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Reference proteome.
FT CHAIN 1..261
FT /note="Cell division protein B"
FT /id="PRO_0000438766"
FT REGION 213..261
FT /note="Winged-helix-like fold"
FT /evidence="ECO:0000305|PubMed:21255729"
SQ SEQUENCE 261 AA; 29694 MW; 996447C0EC2F9E65 CRC64;
MFDKLSIIFN SDRKRKVHLS KAITEISLKL KEQQDRLDEA IRRLRERDKD LFEKVIRSQI
EGDIARATIY AQEISDIRKM IKIIYTAYLA IEKVRLKLDT VQELQGVSLV LFPVMRILGE
LKEQVRGIAP EVALALDSIT SSVNSIAIET GALSEKTFVP TVADEQAKQI MEEAQKMAEV
KVRELLPELP HPPSELPKRV AKQVQSSNKK SLSEDMILNY IKTTGGFIDV DYIAKNFDVS
KDEVFNVLRR LEEKGLIVLE G
