ID H1G6M7_9GAMM Unreviewed; 97 AA.
AC H1G6M7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Cell division protein FtsB {ECO:0000256|HAMAP-Rule:MF_00599};
GN Name=ftsB {ECO:0000256|HAMAP-Rule:MF_00599};
GN ORFNames=ECTPHS_12378 {ECO:0000313|EMBL:EHQ53464.1};
OS Ectothiorhodospira sp. PHS-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=519989 {ECO:0000313|EMBL:EHQ53464.1, ECO:0000313|Proteomes:UP000005314};
RN [1] {ECO:0000313|EMBL:EHQ53464.1, ECO:0000313|Proteomes:UP000005314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHS-1 {ECO:0000313|EMBL:EHQ53464.1,
RC ECO:0000313|Proteomes:UP000005314};
RA Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V.,
RA Hoeft S., Oremland R.S., Stolz J.;
RT "ArxA, a new clade of arsenite oxidase within the DMSO family of molybdenum
RT oxidoreductases.";
RL Submitted (JAN-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHQ53464.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGBG01000034; EHQ53464.1; -; Genomic_DNA.
DR RefSeq; WP_008933031.1; NZ_AGBG01000034.1.
DR AlphaFoldDB; H1G6M7; -.
DR STRING; 519989.ECTPHS_12378; -.
DR PATRIC; fig|519989.5.peg.2429; -.
DR eggNOG; COG2919; Bacteria.
DR OrthoDB; 7061211at2; -.
DR Proteomes; UP000005314; Unassembled WGS sequence.
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 Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00599};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00599};
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_00599};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00599};
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..97
FT /note="Periplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00599"
FT COILED 29..70
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00599"
SQ SEQUENCE 97 AA; 11456 MW; A2733F1074D363FD CRC64;
MKWLITLLLA LFLGLQYKLW FGEGSLVEVW QLRQELEIQR AQNQELRGRN EALEAEVIDL
KTGLEAIEER ARRELGMIAE DEIFFQVVDR HRFGGQR
//