ID   A0A3N4WK78_9PAST        Unreviewed;       469 AA.
AC   A0A3N4WK78;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Cell division protein FtsP {ECO:0000256|HAMAP-Rule:MF_00915};
GN   Name=ftsP {ECO:0000256|HAMAP-Rule:MF_00915};
GN   ORFNames=EDC49_1307 {ECO:0000313|EMBL:RPE93793.1};
OS   Frederiksenia canicola.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Frederiksenia.
OX   NCBI_TaxID=123824 {ECO:0000313|EMBL:RPE93793.1, ECO:0000313|Proteomes:UP000276901};
RN   [1] {ECO:0000313|EMBL:RPE93793.1, ECO:0000313|Proteomes:UP000276901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25797 {ECO:0000313|EMBL:RPE93793.1,
RC   ECO:0000313|Proteomes:UP000276901};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (NOV-2018) 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:0000256|HAMAP-
CC       Rule:MF_00915}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_00915}.
CC       Note=Localizes to the division septum. {ECO:0000256|HAMAP-
CC       Rule:MF_00915}.
CC   -!- SIMILARITY: Belongs to the FtsP family. {ECO:0000256|HAMAP-
CC       Rule:MF_00915}.
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:RPE93793.1}.
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DR   EMBL; RKQT01000002; RPE93793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4WK78; -.
DR   OrthoDB; 9757546at2; -.
DR   Proteomes; UP000276901; Unassembled WGS sequence.
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   CDD; cd13867; CuRO_2_CueO_FtsP; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR   HAMAP; MF_00915; FtsP; 1.
DR   InterPro; IPR011707; Cu-oxidase-like_N.
DR   InterPro; IPR011706; Cu-oxidase_C.
DR   InterPro; IPR045087; Cu-oxidase_fam.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR026589; FtsP.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR48267:SF1; BILIRUBIN OXIDASE; 1.
DR   PANTHER; PTHR48267; CUPREDOXIN SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   SUPFAM; SSF49503; Cupredoxins; 3.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00915};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00915};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_00915};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..469
FT                   /note="Cell division protein FtsP"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017989490"
FT   DOMAIN          54..166
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          357..441
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   469 AA;  53303 MW;  0D7C33F32E6C2AD3 CRC64;
     MNKSRRQFLK RTGLATGFAL VPQAVWAAER PKLVIPPLID VGRGRPVRLD FRPAQTQFDS
     GKLVDVWGVN GQYLAPTVRM KSGDVVRLTY INSLPQPLSV NIQGLLAPTE MVGSIHRQLE
     PNQNWSPILT INQPACTGWY HADSMLNSAF QTYRGLAGLW LIEDAESRKA KLPRKYGVDD
     IPLILQDQLI NTDGVQVLDS QALQFWGKRL FVNGQESPYF DVPRGWVRLR IANASLSRRY
     ELRLDNGKPL YQIATGVGFL AQPLEMESIS VAPSERVELL IDLNEGEKVS LISGQKRGFF
     YKVEQFFADD DELIDNVVVE FRPKGLPSAL NSDAVLPPFN VGDFQLKIAQ ERQFTLRPLD
     RLINQQRFDP KRIDFTVQRG TVERWHLTSN DPIGFTLQGA KLIIETQNNQ KFPHKQLAWR
     DTIWLEKDQE MTVLVRFDHA APETHPFTFG VSDLMLRDRG AMGQFVVKE
//