ID   FTSP_EDWTF              Reviewed;         472 AA.
AC   E0T5V0;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Cell division protein FtsP {ECO:0000255|HAMAP-Rule:MF_00915};
DE   Flags: Precursor;
GN   Name=ftsP {ECO:0000255|HAMAP-Rule:MF_00915}; OrderedLocusNames=ETAF_0171;
OS   Edwardsiella tarda (strain FL6-60).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=718251;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FL6-60;
RA   van Soest J.J., Henkel C.V., Jansen H.J., van den Hondel C.A.M.J.J.,
RA   Bloemberg G.V., Meijer A.H., Spaink H.P.;
RT   "Genome comparisons of Edwardsiella bacteria analysed using deep sequencing
RT   technology.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell division protein that is required for growth during
CC       stress conditions. May be involved in protecting or stabilizing the
CC       divisomal assembly under conditions of stress. {ECO:0000255|HAMAP-
CC       Rule:MF_00915}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00915}.
CC       Note=Localizes to the division septum. {ECO:0000255|HAMAP-
CC       Rule:MF_00915}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the FtsP family. {ECO:0000255|HAMAP-
CC       Rule:MF_00915}.
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DR   EMBL; CP002154; ADM40294.1; -; Genomic_DNA.
DR   RefSeq; WP_012847077.1; NC_017309.1.
DR   AlphaFoldDB; E0T5V0; -.
DR   SMR; E0T5V0; -.
DR   EnsemblBacteria; ADM40294; ADM40294; ETAF_0171.
DR   GeneID; 58256475; -.
DR   KEGG; etd:ETAF_0171; -.
DR   PATRIC; fig|718251.5.peg.172; -.
DR   HOGENOM; CLU_009100_2_4_6; -.
DR   OMA; GMWIIED; -.
DR   Proteomes; UP000002230; Chromosome.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProtKB-UniRule.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.40.420; -; 3.
DR   HAMAP; MF_00915; FtsP; 1.
DR   InterPro; IPR011706; Cu-oxidase_C.
DR   InterPro; IPR045087; Cu-oxidase_fam.
DR   InterPro; IPR011707; Cu-oxidase_N.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR026589; FtsP.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR11709; PTHR11709; 1.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   SUPFAM; SSF49503; SSF49503; 3.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Periplasm; Signal.
FT   SIGNAL          1..32
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00915"
FT   CHAIN           33..472
FT                   /note="Cell division protein FtsP"
FT                   /id="PRO_0000416006"
SQ   SEQUENCE   472 AA;  51330 MW;  4AB57ED7B2B8306B CRC64;
     MSLSRRRFIQ ASGLALCAGG LPLQARASGA QAVLPVPPLL ESRRGQPLFL SLERTHWAFM
     GGRKVGTWGV NGVYLGPTVR VHSGDDVKLI YSNRLSESVA MEVAGLLVPG PLAGGPARQM
     SPGVDWSPVL PIRQAAATLW YHADTPRHMA PQVYSGLAGL WLVEDQYSKN APLPNHYGVD
     DFPLILQDKR LDNFGVPEYD PPSSGGFLGD TLLVNGVQDP YVEVSRGWVR LRLLNASNAR
     RYLLQLSDGR PFFVIASDQG LLPAPLQADT LPLAPGERRE VLIDMSKGEE ISITAGEAAG
     IMDRLRGLFE PSSMLVSTRV LTLRPTGLLP LMTDTLPARL AADPLPEGDV VNNRSIMLGS
     ASSPGINGAL WDPGRIDVQA RQGTWERWTV RADTPQSFYI QGAQFLVKSV NNAPPLVEDR
     GWKDSVWVDG EVSLLVYFPQ PSSEHFPFLF YSGTLELADR GSVGQMVVQP AQ