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Entry: A0A1E7Z3K5_9GAMM
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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
//
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