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Database: UniProt
Entry: A0A0R0DU58_9GAMM
LinkDB: A0A0R0DU58_9GAMM
Original site: A0A0R0DU58_9GAMM 
ID   A0A0R0DU58_9GAMM        Unreviewed;       411 AA.
AC   A0A0R0DU58;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Cell division protein FtsA {ECO:0000256|HAMAP-Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101};
GN   Name=ftsA {ECO:0000256|HAMAP-Rule:MF_02033};
GN   ORFNames=ABB34_07615 {ECO:0000313|EMBL:KRG85695.1};
OS   Stenotrophomonas daejeonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=659018 {ECO:0000313|EMBL:KRG85695.1, ECO:0000313|Proteomes:UP000050940};
RN   [1] {ECO:0000313|EMBL:KRG85695.1, ECO:0000313|Proteomes:UP000050940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16244 {ECO:0000313|EMBL:KRG85695.1,
RC   ECO:0000313|Proteomes:UP000050940};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell division protein that is involved in the assembly of the
CC       Z ring. May serve as a membrane anchor for the Z ring.
CC       {ECO:0000256|HAMAP-Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101}.
CC   -!- SUBUNIT: Self-interacts. Interacts with FtsZ. {ECO:0000256|HAMAP-
CC       Rule:MF_02033}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02033};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_02033};
CC       Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_02033}. Note=Localizes to
CC       the Z ring in an FtsZ-dependent manner. Targeted to the membrane
CC       through a conserved C-terminal amphipathic helix. {ECO:0000256|HAMAP-
CC       Rule:MF_02033}.
CC   -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000256|HAMAP-
CC       Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101}.
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:KRG85695.1}.
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DR   EMBL; LDJP01000042; KRG85695.1; -; Genomic_DNA.
DR   RefSeq; WP_057640654.1; NZ_LDJP01000042.1.
DR   AlphaFoldDB; A0A0R0DU58; -.
DR   STRING; 659018.ABB34_07615; -.
DR   PATRIC; fig|659018.3.peg.1461; -.
DR   OrthoDB; 9810567at2; -.
DR   Proteomes; UP000050940; Unassembled WGS sequence.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.1490.110; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_02033; FtsA; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR020823; Cell_div_FtsA.
DR   InterPro; IPR003494; SHS2_FtsA.
DR   NCBIfam; TIGR01174; ftsA; 1.
DR   PANTHER; PTHR32432:SF4; CELL DIVISION PROTEIN FTSA; 1.
DR   PANTHER; PTHR32432; CELL DIVISION PROTEIN FTSA-RELATED; 1.
DR   Pfam; PF14450; FtsA; 2.
DR   Pfam; PF02491; SHS2_FTSA; 1.
DR   PIRSF; PIRSF003101; FtsA; 1.
DR   SMART; SM00842; FtsA; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_02033};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_02033};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_02033};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050940}.
FT   DOMAIN          10..197
FT                   /note="SHS2"
FT                   /evidence="ECO:0000259|SMART:SM00842"
SQ   SEQUENCE   411 AA;  43951 MW;  83119E3411ECD662 CRC64;
     MNRKGDKSLI VGLDIGTSKV VALVGEYSPG SPIEVIGIGS HESRGLKRGV VVDIESTVQS
     IQRAIEEAEL MAGCEIRSVY ASISGNHVQC RNSQGITPIR EGEVTWGDLD RVLEAAKAVA
     IPADQKILHA IPREYVLDDS QEGIRNPVGM TGVRLEVHAH LVVCAQSAAA NISKCVQKCG
     LQVDDLVLSS LASSVAVLTA DERELGVVMV DMGAGTTDIA VFVQGAICHT ASLPIAGDHV
     TNDIAHMLRT PTPEAEQIKV RYACALAQLA TAEESIQVPS VGDRPPRRMP RASLAQAVQG
     RYEEIFEMVQ AELRRSGFEE MVRAGMVLTG GASKMEGVVE LAEEMLQMPV RVGIPQHVTG
     LGEVVGNPVH ATGVGLLLMG SQIEHPRRPS LPVGRAGTLF NKLKNWFRGE F
//
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