ID   FTSP_SODGM              Reviewed;         473 AA.
AC   Q2NWC3;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Cell division protein FtsP;
DE   Flags: Precursor;
GN   Name=ftsP; OrderedLocusNames=SG0277;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans;
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(2006).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. Note=Localizes to the
CC       division septum. {ECO:0000250}.
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:0000305}.
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DR   EMBL; AP008232; BAE73552.1; -; Genomic_DNA.
DR   RefSeq; WP_011410140.1; NZ_LN854557.1.
DR   AlphaFoldDB; Q2NWC3; -.
DR   SMR; Q2NWC3; -.
DR   STRING; 343509.SG0277; -.
DR   EnsemblBacteria; BAE73552; BAE73552; SG0277.
DR   KEGG; sgl:SG0277; -.
DR   eggNOG; COG2132; Bacteria.
DR   HOGENOM; CLU_009100_2_4_6; -.
DR   OMA; GMWIIED; -.
DR   OrthoDB; 971126at2; -.
DR   Proteomes; UP000001932; 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   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..27
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           28..473
FT                   /note="Cell division protein FtsP"
FT                   /id="PRO_0000416015"
SQ   SEQUENCE   473 AA;  51751 MW;  E36C7AD7B1150F70 CRC64;
     MSLSRRRFIQ ATGATLAASA LPLQAQAAET PVALPIPPLL ESRRGQPLFL TLQRLHWTFA
     AGRRAATWGI NGGYLGPTVR VYNGDDVNII YNNRLTEPVA MTVSGLQVPG TLMGGAARMM
     SPGADWSPVL PIRQTAGTCW YHANTPNRMA PHIYNGLAGL WLVEDAVSKV LPLPNHYGVD
     DFPLIIQDKR LDNFGQPVYN PPASGGFLGD TLLVNGAQSP FVEVSRGWVR LRLLNASNSR
     CYQLQLSDGR AMHVVAGDQG FLPAPVPVIR LSLAPGERRE ILIDMSKGEE VAITAGEAAG
     LMDRVRGFFE PSSILVNTTV LTLKPTGLLP LVTDNLPMRL LSDQLIDGGI SRTREFSLGG
     STPDINGALW NMSRNDFQSL QGSFERWIVH TNTPQAFHIQ GVAFLIKRVN GNTPLPEDQG
     WKDTVWVDNE VELLVWFPQV APDHFPYLYY SQTLEMADRG AAGQFVVRPQ SVG