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Database: UniProt
Entry: Q8E6N9_STRA3
LinkDB: Q8E6N9_STRA3
Original site: Q8E6N9_STRA3 
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
//
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