ID I4VZV1_9GAMM Unreviewed; 225 AA.
AC I4VZV1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Cell division ATP-binding protein FtsE {ECO:0000256|ARBA:ARBA00020019, ECO:0000256|RuleBase:RU365094};
GN Name=ftsE {ECO:0000256|RuleBase:RU365094};
GN ORFNames=UU7_10650 {ECO:0000313|EMBL:EIL92742.1};
OS Rhodanobacter spathiphylli B39.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163407 {ECO:0000313|EMBL:EIL92742.1, ECO:0000313|Proteomes:UP000003226};
RN [1] {ECO:0000313|EMBL:EIL92742.1, ECO:0000313|Proteomes:UP000003226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B39 {ECO:0000313|EMBL:EIL92742.1,
RC ECO:0000313|Proteomes:UP000003226};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
CC -!- FUNCTION: Part of the ABC transporter FtsEX involved in cellular
CC division. Important for assembly or stability of the septal ring.
CC {ECO:0000256|ARBA:ARBA00002579}.
CC -!- SUBUNIT: Homodimer. Forms a membrane-associated complex with FtsX.
CC {ECO:0000256|RuleBase:RU365094}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|RuleBase:RU365094}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU365094}; Cytoplasmic side
CC {ECO:0000256|RuleBase:RU365094}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC {ECO:0000256|RuleBase:RU365094}.
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:EIL92742.1}.
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DR EMBL; AJXT01000030; EIL92742.1; -; Genomic_DNA.
DR RefSeq; WP_007808137.1; NZ_AJXT01000030.1.
DR AlphaFoldDB; I4VZV1; -.
DR STRING; 1163407.UU7_10650; -.
DR PATRIC; fig|1163407.3.peg.2137; -.
DR eggNOG; COG2884; Bacteria.
DR OrthoDB; 9802264at2; -.
DR Proteomes; UP000003226; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR015854; ABC_transpr_LolD-like.
DR InterPro; IPR005286; Cell_div_FtsE.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR02673; FtsE; 1.
DR PANTHER; PTHR24220:SF470; CELL DIVISION ATP-BINDING PROTEIN FTSE; 1.
DR PANTHER; PTHR24220; IMPORT ATP-BINDING PROTEIN; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365094};
KW Cell cycle {ECO:0000256|RuleBase:RU365094};
KW Cell division {ECO:0000256|RuleBase:RU365094, ECO:0000313|EMBL:EIL92742.1};
KW Cell membrane {ECO:0000256|RuleBase:RU365094};
KW Membrane {ECO:0000256|RuleBase:RU365094};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365094};
KW Reference proteome {ECO:0000313|Proteomes:UP000003226}.
FT DOMAIN 2..225
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 225 AA; 24685 MW; 9E5CF1AFFB477D49 CRC64;
MIQFDQVSKR YEGGHEALSQ LSFEVPTGEM AFVTGHSGAG KSTLLKLLGL IERPSHGTIS
VDGKSLAKIR HSGIPKWRRH LGMVFQDHRL LLDRSVFANV ELPLVIGGIA RAERARRVRA
ALEKVGLLAY ERQLPATLST GEQQRVGIAR AIVARPSLLI ADEPTGNLDP QLAVEIMGLF
DEFQQVGTTV LIASHDLPLI KRMKKRVIVL DHGRLVADLA AQEVL
//
