ID DIVIB_ENTF6 Reviewed; 374 AA.
AC F0PBT2;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Cell division protein DivIB {ECO:0000255|HAMAP-Rule:MF_00912};
GN Name=divIB {ECO:0000255|HAMAP-Rule:MF_00912}; OrderedLocusNames=EF62_1429;
OS Enterococcus faecalis (strain 62).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=936153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=62;
RX PubMed=21398545; DOI=10.1128/jb.00183-11;
RA Brede D.A., Snipen L.G., Ussery D.W., Nederbragt A.J., Nes I.F.;
RT "Complete genome sequence of the commensal Enterococcus faecalis 62,
RT isolated from a healthy Norwegian infant.";
RL J. Bacteriol. 193:2377-2378(2011).
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; CP002491; ADX79673.1; -; Genomic_DNA.
DR AlphaFoldDB; F0PBT2; -.
DR KEGG; efl:EF62_1429; -.
DR PATRIC; fig|936153.3.peg.1390; -.
DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.10960; -; 1.
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 PANTHER; PTHR37820; CELL DIVISION PROTEIN DIVIB; 1.
DR PANTHER; PTHR37820:SF1; CELL DIVISION PROTEIN FTSQ; 1.
DR Pfam; PF03799; FtsQ_DivIB_C; 1.
DR Pfam; PF08478; POTRA_1; 1.
DR PROSITE; PS51779; POTRA; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..374
FT /note="Cell division protein DivIB"
FT /id="PRO_0000414765"
FT TOPO_DOM 1..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00912"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00912"
FT TOPO_DOM 125..374
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00912"
FT DOMAIN 126..197
FT /note="POTRA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 42146 MW; E32265A2A1A59FB3 CRC64;
MWKISNENDI FKKRKPLPPK KSEESQPELT PWQKQNQEYL KKQAEEAASK GENEQAEVTI
TLQEQSQEEP QQHLPQETVE EEEHFADRLP NVKKTRNKRL YRRLAFILTC LGTAILVALY
FVSPLSRLSE VTVSGNKSVE SQAIIQQSKL ETGSGLWEQY SNRNYFSANI QKKFPIIKKA
NIKLNGINSF KIDIQEYQIV ALAATKGGYH PILENGKTLA ETTKAAESGK PIFENFKEDK
LIPELMASYN KLPQEIKQGI SEIKYAPSKT NKDLINVYMN DGNRVIVNIS DLSEKMAYYS
QVAEQMDKPG IVDMEVGIFS YPYEKESEET GSEVSEDSAV ENQEVVDPNA GVATDGANNG
TPTNGENQEV QQAE
//
