ID   FTSP_GALAU              Reviewed;         466 AA.
AC   F4HDA7;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 48.
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};
GN   OrderedLocusNames=UMN179_00611;
OS   Gallibacterium anatis (strain UMN179) (Pasteurella anatis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Gallibacterium.
OX   NCBI_TaxID=1005058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMN179;
RX   PubMed=21602325; DOI=10.1128/jb.05177-11;
RA   Johnson T.J., Fernandez-Alarcon C., Bojesen A.M., Nolan L.K., Trampel D.W.,
RA   Seemann T.;
RT   "Complete genome sequence of Gallibacterium anatis strain UMN179, isolated
RT   from a laying hen with peritonitis.";
RL   J. Bacteriol. 193:3676-3677(2011).
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; CP002667; AEC16645.1; -; Genomic_DNA.
DR   RefSeq; WP_013745432.1; NC_015460.1.
DR   AlphaFoldDB; F4HDA7; -.
DR   SMR; F4HDA7; -.
DR   STRING; 1005058.UMN179_00611; -.
DR   PRIDE; F4HDA7; -.
DR   EnsemblBacteria; AEC16645; AEC16645; UMN179_00611.
DR   KEGG; gan:UMN179_00611; -.
DR   PATRIC; fig|1005058.3.peg.599; -.
DR   eggNOG; COG2132; Bacteria.
DR   HOGENOM; CLU_009100_2_4_6; -.
DR   OMA; GMWIIED; -.
DR   OrthoDB; 971126at2; -.
DR   Proteomes; UP000006908; 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..28
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00915"
FT   CHAIN           29..466
FT                   /note="Cell division protein FtsP"
FT                   /id="PRO_0000416008"
SQ   SEQUENCE   466 AA;  52154 MW;  E7AD548F840E52C6 CRC64;
     MGNYSRRRFL QGSLAIVAGN VLPCAAMAAD NPPLWIPPLT SVGRGSPILL NARNVKKAFD
     NNKVDAWGFN GSYLGPTIKM KQNDFLRLTY RNNLSEAIAI NIQGLQANGE VSGSINRNLA
     PNSSWSPIIQ IKQSASTCWY HSDTIGRSAY QSYRGLIGMW IIEDEESKKN LLPNKYGEND
     IPLILQDISL NYDGQQVFNL EKNSFLGKQL FVNGQRNPFI NVARGFIRLR LLNASVSRPY
     YLHLDNQQPF FKIASGLGFL PQPLEQKVLL LAPGERAEIL VNTNQNKPLR LLAGDSANII
     DKVRGWLGMS DHLQNNLVVE LRPQGLASAF AQQKPTLPDA KLGLPLSPQK ERHIHLSTQD
     AMINQRRFDP RRIDIFAQLN SVERWVLTAD QATGFQLQGA KFLIEQQNGE RNKKEMLAWT
     DTVWVEGETR ILVQFDNPSS NSYPFIFGAS NLLLADKGCM GLLVVQ