ID   FTSP_GLAP5              Reviewed;         469 AA.
AC   B8F891;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=HAPS_2087;
OS   Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Glaesserella.
OX   NCBI_TaxID=557723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH0165;
RX   PubMed=19074396; DOI=10.1128/jb.01682-08;
RA   Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA   Jin M., Jin Q., Chen H.;
RT   "Complete genome sequence of Haemophilus parasuis SH0165.";
RL   J. Bacteriol. 191:1359-1360(2009).
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; CP001321; ACL33543.1; -; Genomic_DNA.
DR   RefSeq; WP_015940063.1; NC_011852.1.
DR   AlphaFoldDB; B8F891; -.
DR   SMR; B8F891; -.
DR   STRING; 557723.HAPS_2087; -.
DR   EnsemblBacteria; ACL33543; ACL33543; HAPS_2087.
DR   KEGG; hap:HAPS_2087; -.
DR   HOGENOM; CLU_009100_2_4_6; -.
DR   OMA; GMWIIED; -.
DR   Proteomes; UP000006743; 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   InterPro; IPR019546; TAT_signal_bac_arc.
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   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00915"
FT   CHAIN           28..469
FT                   /note="Cell division protein FtsP"
FT                   /id="PRO_0000416010"
SQ   SEQUENCE   469 AA;  53347 MW;  BCD7089969DCCDB6 CRC64;
     MKLSRRQFLQ RSTLAGVATV TPTSLWAKNR PSLTIPPMIE VGRGRPVRLD FRPAQTQFNK
     GKLVDVWGVN GRYLAPTVRV KSGDFVKLTY TNNLPQALSI NIQGLQAPTE MIGSIHRAID
     KNSSWSPILS VNQSACTAWY HADTMLNSAF QVYRGLAGLW IIEDSESRKA SLPNKYGVND
     IPLILQDQLI NSDGIQVIDT QTNQFFGKRL FVNGQESPYF DVPRGWVRLR IANASLSRHY
     DLRLDNGKPL YLIATGIGFL ADMVEMEHIS LAPSERIEVL VDLNEGDKVS LITGKKRDFF
     DEIGKLFKDN NELNDNVVLE FRPEGLPSAL NVTPKLPPFN VEEFNLKITQ ERKINLRPQD
     RLINHQRFDP KRIDFTVKKG TVERWYLTTT EEVGFTLQGA KFMVETRNRQ AVPHKQLAWR
     DCVWLEPTQE TTLLVKFEHT ASEQQPFTFG VSDLMLRDRG CMGQFVVAE