(data stored in ACNUC9543 zone)

SWISSPROT: A0A0E1NPB1_YERPA

ID   A0A0E1NPB1_YERPA        Unreviewed;       248 AA.
AC   A0A0E1NPB1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   05-DEC-2018, entry version 23.
DE   RecName: Full=Cell division protein FtsN {ECO:0000256|HAMAP-Rule:MF_02039};
GN   Name=ftsN {ECO:0000256|HAMAP-Rule:MF_02039};
GN   OrderedLocusNames=YPA_0257 {ECO:0000313|EMBL:ABG12226.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12226.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12226.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12226.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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
CC       and 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
CC       domain. {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
CC       division protein FtsA and via the periplasmic SPOR domain.
CC       {ECO:0000256|HAMAP-Rule:MF_02039}.
CC   -!- SIMILARITY: Belongs to the FtsN family. {ECO:0000256|HAMAP-
CC       Rule:MF_02039}.
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DR   EMBL; CP000308; ABG12226.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABG12226; ABG12226; YPA_0257.
DR   EnsemblBacteria; AJJ78784; AJJ78784; CH58_3102.
DR   KEGG; ypa:YPA_0257; -.
DR   PATRIC; fig|360102.15.peg.3253; -.
DR   KO; K03591; -.
DR   OMA; RPEEVWS; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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; -; 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   Pfam; PF05036; SPOR; 1.
DR   SUPFAM; SSF110997; SSF110997; 1.
DR   TIGRFAMs; TIGR02223; ftsN; 1.
DR   PROSITE; PS51724; SPOR; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0E1NPB1.
DR   SWISS-2DPAGE; A0A0E1NPB1.
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_02039};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_02039,
KW   ECO:0000313|EMBL:ABG12226.1};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02039};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_02039};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_02039};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_02039};
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   DISULFID    181    241       {ECO:0000256|HAMAP-Rule:MF_02039}.
SQ   SEQUENCE   248 AA;  26841 MW;  48E23AB523761AB8 CRC64;
     MALAVALLVV FVGGLYFITH NKPGELPLLP NHDPRTGNGL PPKPEERWRY IKELENRQIG
     VPMPTEPSAG GEVNAKTELT NEQRQLLEQM QADMRQQPTQ LSEVPYNQGM QQVPRSAVTI
     KPPATSVQPQ PVTPPRQTTI PVQPQAPAPV RTPPAAPVTQ AVTPPKVEKE KEKTQRWMVQ
     CGSFKAVDQA ESIRAQLAFA GIESRITSGG GWNRVVLGPY NSKAAADKAL QRLQGAGQSG
     CIPLSVGG
//

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