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Database: UniProt
Entry: A0A0S1Y1L9_9BORD
LinkDB: A0A0S1Y1L9_9BORD
Original site: A0A0S1Y1L9_9BORD 
ID   A0A0S1Y1L9_9BORD        Unreviewed;       136 AA.
AC   A0A0S1Y1L9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Cell division protein FtsB {ECO:0000256|HAMAP-Rule:MF_00599};
GN   Name=ftsB {ECO:0000256|HAMAP-Rule:MF_00599};
GN   ORFNames=ASB57_13740 {ECO:0000313|EMBL:ALM83890.1};
OS   Bordetella sp. N.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM83890.1, ECO:0000313|Proteomes:UP000064621};
RN   [1] {ECO:0000313|EMBL:ALM83890.1, ECO:0000313|Proteomes:UP000064621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N {ECO:0000313|EMBL:ALM83890.1,
RC   ECO:0000313|Proteomes:UP000064621};
RA   Hou L.;
RT   "Draft genome of Bordetella sp. N.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential cell division protein. May link together the
CC       upstream cell division proteins, which are predominantly cytoplasmic,
CC       with the downstream cell division proteins, which are predominantly
CC       periplasmic. {ECO:0000256|HAMAP-Rule:MF_00599}.
CC   -!- SUBUNIT: Part of a complex composed of FtsB, FtsL and FtsQ.
CC       {ECO:0000256|HAMAP-Rule:MF_00599}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00599}; Single-pass type II membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_00599}. Note=Localizes to the division
CC       septum. {ECO:0000256|HAMAP-Rule:MF_00599}.
CC   -!- SIMILARITY: Belongs to the FtsB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00599}.
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DR   EMBL; CP013111; ALM83890.1; -; Genomic_DNA.
DR   RefSeq; WP_057652735.1; NZ_CP013111.1.
DR   AlphaFoldDB; A0A0S1Y1L9; -.
DR   STRING; 1746199.ASB57_13740; -.
DR   OrthoDB; 7061211at2; -.
DR   Proteomes; UP000064621; 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   HAMAP; MF_00599; FtsB; 1.
DR   InterPro; IPR023081; Cell_div_FtsB.
DR   InterPro; IPR007060; FtsL/DivIC.
DR   PANTHER; PTHR37485; CELL DIVISION PROTEIN FTSB; 1.
DR   PANTHER; PTHR37485:SF1; CELL DIVISION PROTEIN FTSB; 1.
DR   Pfam; PF04977; DivIC; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00599};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00599,
KW   ECO:0000313|EMBL:ALM83890.1};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00599};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00599};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00599};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064621};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00599};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00599}.
FT   TOPO_DOM        1..3
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00599"
FT   TOPO_DOM        22..136
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00599"
FT   REGION          89..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   136 AA;  14514 MW;  C501282C84E3E98F CRC64;
     MRLLFLVLFV LVGLIQYPLW AGKGGWFKVW DLQKQLAAQR ETNDGLRARN NALDAEVHDL
     QSGTGAIEER ARSELGMMRD GEIFVQILPQ NTAPPPGGAS VATPDTVAAT PAPASRPAAA
     APNRPATAPA RPAARH
//
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