ID G5NKX1_SALET Unreviewed; 307 AA.
AC G5NKX1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Cell division protein FtsN {ECO:0000256|HAMAP-Rule:MF_02039};
GN Name=ftsN {ECO:0000256|HAMAP-Rule:MF_02039};
GN ORFNames=LTSEINV_5809 {ECO:0000313|EMBL:EHC49053.1};
OS Salmonella enterica subsp. enterica serovar Inverness str. R8-3668.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913075 {ECO:0000313|EMBL:EHC49053.1, ECO:0000313|Proteomes:UP000003532};
RN [1] {ECO:0000313|EMBL:EHC49053.1, ECO:0000313|Proteomes:UP000003532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R8-3668 {ECO:0000313|EMBL:EHC49053.1,
RC ECO:0000313|Proteomes:UP000003532};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
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:EHC49053.1}.
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DR EMBL; AFCO01001893; EHC49053.1; -; Genomic_DNA.
DR AlphaFoldDB; G5NKX1; -.
DR PATRIC; fig|913075.3.peg.4540; -.
DR Proteomes; UP000003532; 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:EHC49053.1};
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 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 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02039"
FT DOMAIN 230..304
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
FT REGION 61..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 240..300
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02039"
SQ SEQUENCE 307 AA; 34022 MW; FAC2A21DCA821168 CRC64;
MPAVSPAMVA IAAAVLVTFI GGLYFITHHK KEESETLQNQ KVTGNGLPPK PEERWRYIKE
LESRQPGVRT PTEPSAASAG GEVMKTEPSA GGEVMNPNQL TSEQRQLLEQ MQADMRQQPT
QLNEVPWNEQ TPEQRQQTLQ RQRQAQQQQW TQTQPVQQPR TQPRVNEQPQ TRTVQSAPAQ
PARQSQPPKQ TASQQPYQDL LQTPAHTSAA APKAAPITRA PETPKATAEK KDERRWMVQC
GSFKGAEQAE SVRAQLAFEG FDSKITTNNG WNRVVIGPVK GKENADSTIN RLKMAGHTNC
IRLATGG
//
