ID G7UP86_PSEUP Unreviewed; 123 AA.
AC G7UP86;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Cell division protein FtsB {ECO:0000256|HAMAP-Rule:MF_00599};
GN Name=ftsB {ECO:0000256|HAMAP-Rule:MF_00599,
GN ECO:0000313|EMBL:AER56780.1};
GN OrderedLocusNames=DSC_10680 {ECO:0000313|EMBL:AER56780.1};
OS Pseudoxanthomonas spadix (strain BD-a59).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER56780.1, ECO:0000313|Proteomes:UP000005870};
RN [1] {ECO:0000313|EMBL:AER56780.1, ECO:0000313|Proteomes:UP000005870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD-a59 {ECO:0000313|EMBL:AER56780.1,
RC ECO:0000313|Proteomes:UP000005870};
RX PubMed=22207748; DOI=10.1128/JB.06436-11;
RA Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT spadix BD-a59.";
RL J. Bacteriol. 194:544-544(2012).
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; CP003093; AER56780.1; -; Genomic_DNA.
DR AlphaFoldDB; G7UP86; -.
DR STRING; 1045855.DSC_10680; -.
DR KEGG; psd:DSC_10680; -.
DR eggNOG; COG2919; Bacteria.
DR HOGENOM; CLU_134863_5_0_6; -.
DR OrthoDB; 7061211at2; -.
DR Proteomes; UP000005870; 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:AER56780.1};
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:UP000005870};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00599};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00599}.
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00599"
FT TOPO_DOM 25..123
FT /note="Periplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00599"
FT REGION 93..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 123 AA; 13291 MW; 44333FE3D8265C77 CRC64;
MAKPRWLLLV LVLLLVFLQY HLWFGRGSSG EVIAMRAQVA SQVRENQGLQ QRNAALAAEV
EDLKSGEAAV EERARSELGM IKPGEKFYRV VDTPAGQAGM SGDQLPAVPQ AAQDPAPAQA
EGH
//