ID A0A1E7Z3K5_9GAMM Unreviewed; 297 AA.
AC A0A1E7Z3K5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Cell division protein FtsN {ECO:0000256|HAMAP-Rule:MF_02039};
GN Name=ftsN {ECO:0000256|HAMAP-Rule:MF_02039,
GN ECO:0000313|EMBL:RAP72342.1};
GN ORFNames=ACZ87_00823 {ECO:0000313|EMBL:RAP72342.1}, BBW68_05840
GN {ECO:0000313|EMBL:OFC63314.1};
OS Candidatus Erwinia dacicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=252393 {ECO:0000313|EMBL:OFC63314.1, ECO:0000313|Proteomes:UP000243534};
RN [1] {ECO:0000313|EMBL:OFC63314.1, ECO:0000313|Proteomes:UP000243534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL {ECO:0000313|EMBL:OFC63314.1,
RC ECO:0000313|Proteomes:UP000243534};
RA Yuval B.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RAP72342.1, ECO:0000313|Proteomes:UP000244334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oroville {ECO:0000313|EMBL:RAP72342.1,
RC ECO:0000313|Proteomes:UP000244334};
RA Estes A.M., Hearn D.J., Agarwal S., Pierson E.A., Dunning-Hotopp J.C.;
RT "Genomes of the Obligate Erwinia dacicola and Facultative Enterobacter sp.
RT OLF Endosymbionts of the Olive Fruit fly, Bactrocera oleae.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential cell division protein that activates septal
CC peptidoglycan synthesis and constriction of the cell. Acts on both
CC sides of the membrane, via interaction with FtsA in the cytoplasm and
CC interaction with the FtsQBL complex in the periplasm. These
CC interactions may induce a conformational switch in both FtsA and
CC FtsQBL, leading to septal peptidoglycan synthesis by FtsI and
CC associated synthases. {ECO:0000256|HAMAP-Rule:MF_02039}.
CC -!- SUBUNIT: Interacts with FtsA via its N-terminal cytoplasmic domain.
CC {ECO:0000256|HAMAP-Rule:MF_02039}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02039}; Single-pass type II membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_02039}. Note=Localizes to the septum.
CC Localizes to the midcell via interaction with the early cell division
CC protein FtsA and via the periplasmic SPOR domain. {ECO:0000256|HAMAP-
CC Rule:MF_02039}.
CC -!- SIMILARITY: Belongs to the FtsN family. {ECO:0000256|HAMAP-
CC Rule:MF_02039}.
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:OFC63314.1}.
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DR EMBL; MAYS01000103; OFC63314.1; -; Genomic_DNA.
DR EMBL; LJAM02000042; RAP72342.1; -; Genomic_DNA.
DR RefSeq; WP_070133957.1; NZ_MAYS01000103.1.
DR AlphaFoldDB; A0A1E7Z3K5; -.
DR OrthoDB; 8558195at2; -.
DR Proteomes; UP000243534; Unassembled WGS sequence.
DR Proteomes; UP000244334; 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:0042834; F:peptidoglycan binding; IEA:InterPro.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.1070; Sporulation related repeat; 1.
DR HAMAP; MF_02039; FtsN_entero; 1.
DR InterPro; IPR011930; FtsN.
DR InterPro; IPR007730; SPOR-like_dom.
DR InterPro; IPR036680; SPOR-like_sf.
DR NCBIfam; TIGR02223; ftsN; 1.
DR PANTHER; PTHR38687; CELL DIVISION PROTEIN DEDD-RELATED; 1.
DR PANTHER; PTHR38687:SF2; CELL DIVISION PROTEIN FTSN; 1.
DR Pfam; PF05036; SPOR; 1.
DR SUPFAM; SSF110997; Sporulation related repeat; 1.
DR PROSITE; PS51724; SPOR; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_02039};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_02039,
KW ECO:0000313|EMBL:OFC63314.1};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02039};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02039};
KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_02039};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_02039};
KW Reference proteome {ECO:0000313|Proteomes:UP000244334};
KW Septation {ECO:0000256|HAMAP-Rule:MF_02039};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02039};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02039}.
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02039"
FT DOMAIN 217..296
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 227..287
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02039"
SQ SEQUENCE 297 AA; 33135 MW; 17812F730955569B CRC64;
MAQKDYVGRG RSTGTRRKKT DSRSKKRSSG SDVPKIMVVL AVAVLVTFIG GLWFIAHHKK
EDVPVDMPVI PDHKATGNGL PPKPEERWRY IKELENRQLG VPTPTEPTSG GEAHSQTQLT
DEQRHLLDQM QADMRHQPTQ LNEVPWNEQI PAQRQQQTQL QQQSRMPQQP VRTQPQQAQQ
PAAPITPVTH GPVRQQLKQE TTAAAPKVET KPKKAEKING QRWMVQCGSF KGTEQAQSIR
AQLAFEGFES RITTGGGWNR VVMGPYNNRS GVDSTLKRLR GSGHSNCIPL SVGVETL
//