FTSB_BORPD
ID FTSB_BORPD Reviewed; 111 AA.
AC A9IIP9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Cell division protein FtsB {ECO:0000255|HAMAP-Rule:MF_00599};
GN Name=ftsB {ECO:0000255|HAMAP-Rule:MF_00599}; OrderedLocusNames=Bpet1803;
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
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:0000255|HAMAP-Rule:MF_00599}.
CC -!- SUBUNIT: Part of a complex composed of FtsB, FtsL and FtsQ.
CC {ECO:0000255|HAMAP-Rule:MF_00599}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00599}; Single-pass type II membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00599}. Note=Localizes to the division
CC septum. {ECO:0000255|HAMAP-Rule:MF_00599}.
CC -!- SIMILARITY: Belongs to the FtsB family. {ECO:0000255|HAMAP-
CC Rule:MF_00599}.
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DR EMBL; AM902716; CAP42142.1; -; Genomic_DNA.
DR AlphaFoldDB; A9IIP9; -.
DR SMR; A9IIP9; -.
DR STRING; 94624.Bpet1803; -.
DR EnsemblBacteria; CAP42142; CAP42142; Bpet1803.
DR KEGG; bpt:Bpet1803; -.
DR eggNOG; COG2919; Bacteria.
DR OMA; YELGMVK; -.
DR Proteomes; UP000001225; Chromosome.
DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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; PTHR37485; 1.
DR Pfam; PF04977; DivIC; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Coiled coil;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..111
FT /note="Cell division protein FtsB"
FT /id="PRO_1000129921"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00599"
FT TRANSMEM 4..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00599"
FT TOPO_DOM 22..111
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00599"
FT REGION 88..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 31..62
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00599"
SQ SEQUENCE 111 AA; 12123 MW; 6183ADE38C9103FB CRC64;
MRLLFLVLLV LLGLIQYPLW LGKGGWFKVW DLQRQVAAQH ETNDGLRARN AALEAEVRDL
ATGVGAIEER ARSELGMMRE GEVFVQIVPP GTPVPQPAPG APGQTASAPR R