ID A0A097QXJ3_HAFAL Unreviewed; 292 AA.
AC A0A097QXJ3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Cell division protein FtsN {ECO:0000256|HAMAP-Rule:MF_02039};
GN Name=ftsN {ECO:0000256|HAMAP-Rule:MF_02039};
GN ORFNames=AT03_01450 {ECO:0000313|EMBL:AIU71195.1};
OS Hafnia alvei FB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU71195.1, ECO:0000313|Proteomes:UP000029986};
RN [1] {ECO:0000313|EMBL:AIU71195.1, ECO:0000313|Proteomes:UP000029986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB1 {ECO:0000313|EMBL:AIU71195.1,
RC ECO:0000313|Proteomes:UP000029986};
RX PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA Tan J.Y., Yin W.F., Chan K.G.;
RT "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT pathogenesis: a draft genome perspective.";
RL Gut Pathog. 6:29-29(2014).
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}.
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DR EMBL; CP009706; AIU71195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A097QXJ3; -.
DR KEGG; hav:AT03_01450; -.
DR PATRIC; fig|1453496.5.peg.299; -.
DR eggNOG; COG3087; Bacteria.
DR HOGENOM; CLU_058902_0_0_6; -.
DR Proteomes; UP000029986; Chromosome.
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:AIU71195.1};
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:UP000029986};
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 DOMAIN 215..290
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
FT REGION 57..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 225..285
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02039"
SQ SEQUENCE 292 AA; 31849 MW; 22C6FAC65FAB81B3 CRC64;
MVVVALGVLV TFAAGLYFLT HHKPDSDELL PTQAKHAGNG LPPKPEERWR YIKELENRQV
GVATPTDPTS SAATAPTQQP QLTAEQRQLL DQMQSDMRQQ PTQLSEVPYN DQTQIARRAP
QNSRMPDQTY TQQQPVTSSQ PRNPFSQQNT APSQPRQTTT EPARPVRTAP PVQATQPPVQ
QPHKEKPAPV TSVAEQPAPA KETKTDKAAE KAPEKENAQK WMVQCGSFRS TDQAESVRAQ
LAFGGVESRI TAGGGWNRVL LGPYTSRASA DKMLQRLKGD GMSGCIALSV GG
//
