ID   DIVIB_GEOKA             Reviewed;         261 AA.
AC   Q5L0X5;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Cell division protein DivIB {ECO:0000255|HAMAP-Rule:MF_00912};
GN   Name=divIB {ECO:0000255|HAMAP-Rule:MF_00912}; OrderedLocusNames=GK1120;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
RN   [2]
RP   STRUCTURE BY NMR OF 117-233, AND DOMAIN.
RX   PubMed=16618922; DOI=10.1073/pnas.0601397103;
RA   Robson S.A., King G.F.;
RT   "Domain architecture and structure of the bacterial cell division protein
RT   DivIB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6700-6705(2006).
CC   -!- FUNCTION: Cell division protein that may be involved in stabilizing or
CC       promoting the assembly of the division complex. {ECO:0000255|HAMAP-
CC       Rule:MF_00912}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00912};
CC       Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_00912}.
CC       Note=Localizes to the division septum. {ECO:0000255|HAMAP-
CC       Rule:MF_00912}.
CC   -!- DOMAIN: The extracellular region contains three distinct subdomains: a
CC       membrane proximal alpha domain, a central beta domain and a C-terminal
CC       gamma domain. The alpha domain might serve as a chaperone that
CC       stabilizes FtsL. The gamma domain is required for interaction with
CC       other divisomal proteins. The beta domain might modulate protein-
CC       protein interactions of the flanking alpha and gamma domains.
CC       {ECO:0000269|PubMed:16618922}.
CC   -!- SIMILARITY: Belongs to the FtsQ/DivIB family. DivIB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00912}.
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DR   EMBL; BA000043; BAD75405.1; -; Genomic_DNA.
DR   PDB; 1YR1; NMR; -; A=117-233.
DR   PDB; 2ALJ; NMR; -; A=117-233.
DR   PDBsum; 1YR1; -.
DR   PDBsum; 2ALJ; -.
DR   AlphaFoldDB; Q5L0X5; -.
DR   BMRB; Q5L0X5; -.
DR   SMR; Q5L0X5; -.
DR   STRING; 235909.GK1120; -.
DR   EnsemblBacteria; BAD75405; BAD75405; GK1120.
DR   KEGG; gka:GK1120; -.
DR   eggNOG; COG1589; Bacteria.
DR   HOGENOM; CLU_046278_2_1_9; -.
DR   OMA; YMNDGNE; -.
DR   EvolutionaryTrace; Q5L0X5; -.
DR   Proteomes; UP000001172; Chromosome.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   DisProt; DP02323; -.
DR   HAMAP; MF_00912; DivIB; 1.
DR   InterPro; IPR005548; Cell_div_FtsQ/DivIB_C.
DR   InterPro; IPR026580; DivIB.
DR   InterPro; IPR034746; POTRA.
DR   InterPro; IPR013685; POTRA_FtsQ_type.
DR   Pfam; PF03799; FtsQ; 1.
DR   Pfam; PF08478; POTRA_1; 1.
DR   PROSITE; PS51779; POTRA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cell membrane; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..261
FT                   /note="Cell division protein DivIB"
FT                   /id="PRO_0000414769"
FT   TOPO_DOM        1..27
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00912"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00912"
FT   TOPO_DOM        49..261
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00912"
FT   DOMAIN          50..118
FT                   /note="POTRA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT   REGION          47..117
FT                   /note="Alpha"
FT   REGION          118..230
FT                   /note="Beta"
FT   REGION          231..260
FT                   /note="Gamma"
FT   STRAND          120..126
FT                   /evidence="ECO:0007829|PDB:1YR1"
FT   STRAND          129..134
FT                   /evidence="ECO:0007829|PDB:1YR1"
FT   HELIX           141..143
FT                   /evidence="ECO:0007829|PDB:2ALJ"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:1YR1"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:1YR1"
FT   HELIX           161..173
FT                   /evidence="ECO:0007829|PDB:1YR1"
FT   HELIX           176..180
FT                   /evidence="ECO:0007829|PDB:1YR1"
FT   STRAND          183..187
FT                   /evidence="ECO:0007829|PDB:1YR1"
FT   STRAND          196..200
FT                   /evidence="ECO:0007829|PDB:1YR1"
FT   STRAND          206..213
FT                   /evidence="ECO:0007829|PDB:1YR1"
FT   HELIX           214..219
FT                   /evidence="ECO:0007829|PDB:1YR1"
FT   HELIX           222..230
FT                   /evidence="ECO:0007829|PDB:1YR1"
SQ   SEQUENCE   261 AA;  29714 MW;  F7CC719371AD33D7 CRC64;
     MEKGKVVVLE DRVPKLKERR RQKANRRLIA YLSFFFLFIL CVLYFQSPLG AVGHVEVSGN
     RHLTAERIIS LSGITKRTSF WKVNEQNVEK KLTRHPEIKE ATVEKQLPNT IAIHVREWRR
     IAYVYDRQTF FPLLENGRLL KQEGTKTAPS DAPVLVGWKD GDAIAEMTGQ LAELPAAVLG
     AMSEIHYKPT REYEDRVIVY MNDGYEVSAT IRQFADKLSH YPAIAAALDR NVKGVIHLEV
     GSYFVPYSPP KKEDGDETTS P