ID T1ZGK2_STRIT Unreviewed; 349 AA.
AC T1ZGK2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Cell division protein DivIB {ECO:0000256|HAMAP-Rule:MF_00912};
GN Name=divIB {ECO:0000256|HAMAP-Rule:MF_00912,
GN ECO:0000313|EMBL:AGU76612.1};
GN ORFNames=SIR_1252 {ECO:0000313|EMBL:AGU76612.1};
OS Streptococcus intermedius B196.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=862967 {ECO:0000313|EMBL:AGU76612.1, ECO:0000313|Proteomes:UP000016233};
RN [1] {ECO:0000313|EMBL:AGU76612.1, ECO:0000313|Proteomes:UP000016233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B196 {ECO:0000313|EMBL:AGU76612.1,
RC ECO:0000313|Proteomes:UP000016233};
RX PubMed=24341328; DOI=10.1186/1471-2164-14-895;
RA Olson A.B., Kent H., Sibley C.D., Grinwis M.E., Mabon P., Ouellette C.,
RA Tyson S., Graham M., Tyler S.D., Van Domselaar G., Surette M.G.,
RA Corbett C.R.;
RT "Phylogenetic relationship and virulence inference of Streptococcus
RT Anginosus Group: curated annotation and whole-genome comparative analysis
RT support distinct species designation.";
RL BMC Genomics 14:895-895(2013).
CC -!- FUNCTION: Cell division protein that may be involved in stabilizing or
CC promoting the assembly of the division complex. {ECO:0000256|HAMAP-
CC Rule:MF_00912}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00912};
CC Single-pass type II membrane protein {ECO:0000256|HAMAP-Rule:MF_00912}.
CC Note=Localizes to the division septum. {ECO:0000256|HAMAP-
CC Rule:MF_00912}.
CC -!- SIMILARITY: Belongs to the FtsQ/DivIB family. DivIB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00912}.
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DR EMBL; CP003857; AGU76612.1; -; Genomic_DNA.
DR RefSeq; WP_021003023.1; NZ_UZBH01000003.1.
DR AlphaFoldDB; T1ZGK2; -.
DR KEGG; sib:SIR_1252; -.
DR PATRIC; fig|862967.3.peg.1267; -.
DR eggNOG; COG1589; Bacteria.
DR HOGENOM; CLU_046278_1_1_9; -.
DR OrthoDB; 1819027at2; -.
DR Proteomes; UP000016233; Chromosome.
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 Gene3D; 3.10.20.310; membrane protein fhac; 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 {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_00912};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00912};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00912};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00912};
KW Reference proteome {ECO:0000313|Proteomes:UP000016233};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00912};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00912}.
FT TRANSMEM 125..146
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00912"
FT DOMAIN 150..221
FT /note="POTRA"
FT /evidence="ECO:0000259|PROSITE:PS51779"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..93
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 349 AA; 40329 MW; 9AC4AE0F4CD4E328 CRC64;
MTKKKQKEQK DNGTENLSEW QKRNKEYLEK KAQEEAEKEK ELAEQKKQHL LNYEKLDTDE
EEAKPEETSD IQEAESEETE EPTETEFSEE EQDKSLENEN LKKEEKSEAK QTKREAKEKI
ALRHVYRAFP VLFFSSILLI LAVYFISPYS KLKNIEVTGN KHLSKTEVLA ASSIQKNDYT
LTTYLSQKAH AKNIKLSSLW VEKAEIVYQF PVTFKIKVTE YRVVAYDYSG EQYFPVLSSG
EEISSPVKKS QLPKSYIRLD FSDKAMLKKF VQQLSGISDT IKSEIQTVQH TPSKATEDLL
TITMTDGNKV LVPLSEVAKK LPYYEKIKPQ LTETSVVDME VGIFSYRIS
//
