DIVIB_STRGC
ID DIVIB_STRGC Reviewed; 397 AA.
AC A8AW16;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Cell division protein DivIB {ECO:0000255|HAMAP-Rule:MF_00912};
GN Name=divIB {ECO:0000255|HAMAP-Rule:MF_00912}; OrderedLocusNames=SGO_0673;
OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS DL1 / V288).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=467705;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX PubMed=17720781; DOI=10.1128/jb.01023-07;
RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT to competence signaling peptide.";
RL J. Bacteriol. 189:7799-7807(2007).
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 -!- SIMILARITY: Belongs to the FtsQ/DivIB family. DivIB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00912}.
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DR EMBL; CP000725; ABV09429.1; -; Genomic_DNA.
DR RefSeq; WP_012000148.1; NC_009785.1.
DR AlphaFoldDB; A8AW16; -.
DR STRING; 467705.SGO_0673; -.
DR EnsemblBacteria; ABV09429; ABV09429; SGO_0673.
DR KEGG; sgo:SGO_0673; -.
DR eggNOG; COG1589; Bacteria.
DR HOGENOM; CLU_046278_1_1_9; -.
DR OMA; NHINTAT; -.
DR Proteomes; UP000001131; 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 HAMAP; MF_00912; DivIB; 1.
DR InterPro; IPR026580; DivIB.
DR InterPro; IPR034746; POTRA.
DR InterPro; IPR013685; POTRA_FtsQ_type.
DR Pfam; PF08478; POTRA_1; 1.
DR PROSITE; PS51779; POTRA; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..397
FT /note="Cell division protein DivIB"
FT /id="PRO_0000414788"
FT TOPO_DOM 1..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00912"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00912"
FT TOPO_DOM 160..397
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00912"
FT DOMAIN 160..231
FT /note="POTRA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT REGION 24..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..102
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 45335 MW; A01E6FC16C7F5C04 CRC64;
MTTKDKGDQK ELQKYLSEWQ KRHQEYLEKK SQEKASETDE EERNAEPLET SESAGTKETD
NSEDEKEDQT QDQASDDDET NESEESEDVE EPEEENIEES SDVSEDRTEK FIGQADVGIE
KEAKRDKPRI ERIHLYRALP VLVISSLLIL LSLYFITPLG SLKNLVVTGN ERVTQDEIIK
ATQIDSRDYT LTTFLNRNQY ANNLKKANSW IEKAEISYQF PITFKIQVTE YKILAYEAST
GNIYPVISNG TVINQPVKKE ALPENYMRLN LSDKAKVKKL VQELSDVPDS IKNEIQTVDL
TPSKATKDLL TLTMRDEHKI IVPLSDIHKK LPYYSRVHPL LTEPSIVDME AGIFSYSASL
VQKEEQDQEQ EKEESSEETV PGETEAAPSD VTDETNN