ID Q8E6N9_STRA3 Unreviewed; 378 AA.
AC Q8E6N9;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Cell division protein DivIB {ECO:0000256|HAMAP-Rule:MF_00912};
GN Name=divIB {ECO:0000256|HAMAP-Rule:MF_00912};
GN OrderedLocusNames=gbs0524 {ECO:0000313|EMBL:CAD46168.1};
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110 {ECO:0000313|EMBL:CAD46168.1};
RN [1] {ECO:0000313|EMBL:CAD46168.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316 {ECO:0000313|EMBL:CAD46168.1};
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
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; AL766845; CAD46168.1; -; Genomic_DNA.
DR RefSeq; WP_001124855.1; NC_004368.1.
DR AlphaFoldDB; Q8E6N9; -.
DR GeneID; 66885460; -.
DR KEGG; san:gbs0524; -.
DR eggNOG; COG1589; Bacteria.
DR HOGENOM; CLU_046278_1_0_9; -.
DR Proteomes; UP000000823; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00912};
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 101..121
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00912"
FT DOMAIN 122..193
FT /note="POTRA"
FT /evidence="ECO:0000259|PROSITE:PS51779"
FT REGION 321..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 17..44
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 337..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 43354 MW; 88332F78EE2C8399 CRC64;
MPKKKSDTPE KEEVVLTEWQ KRNLEFLKKR KEDEEEQKRI NEKLRLDKRS KLNISSPEEP
QNTTKIKKLH FPKISKPKIE KKQKKEKIVN SLAKTNRIRT APIFVVAFLV ILVSVFLLTP
FSKQKTITVS GNQHTPDDIL IEKTNIQKND YFFSLIFKHK AIEQRLAAED VWVKTAQMTY
QFPNKFHIQV QENKIIAYAH TKQGYQPVLE TGKKADPVNS SELPKHFLTI NLDKEDSIKL
LIKDLKALDP DLISEIQVIS LADSKTTPDL LLLDMHDGNS IRIPLSKFKE RLPFYKQIKK
NLKEPSIVDM EVGVYTTTST IESTPVKAED TKNKSTDKTQ TQNGQVAENS QGQTNNSNTN
QQGQQIATEQ APNPQNVN
//