ID   FTSP_PASMU              Reviewed;         468 AA.
AC   Q9CPE1;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 109.
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=PM0104;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02188.1; -; Genomic_DNA.
DR   RefSeq; WP_010906483.1; NC_002663.1.
DR   AlphaFoldDB; Q9CPE1; -.
DR   SMR; Q9CPE1; -.
DR   STRING; 747.DR93_1969; -.
DR   EnsemblBacteria; AAK02188; AAK02188; PM0104.
DR   KEGG; pmu:PM0104; -.
DR   PATRIC; fig|272843.6.peg.107; -.
DR   HOGENOM; CLU_009100_2_4_6; -.
DR   OMA; GMWIIED; -.
DR   Proteomes; UP000000809; 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:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.40.420; -; 3.
DR   HAMAP; MF_00915; FtsP; 1.
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; 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; Reference proteome; Signal.
FT   SIGNAL          1..33
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00915"
FT   CHAIN           34..468
FT                   /note="Cell division protein FtsP"
FT                   /id="PRO_0000416011"
SQ   SEQUENCE   468 AA;  52457 MW;  F83D5E95AEB1083B CRC64;
     MDNPARRQFF KTSLIATALS ALPSSLLAAT RQALRIPPLL ETRRGKPIFL SLDSVQYPLE
     MGKTVEVWGF NGHYLGPTIK IRKGDFAKLN YRNNLPQGVS MSIQGLQASG ELLGGVGRVL
     QPKETWSPII PITQAASTCW YHSVSLANSA YQTYRGLAGM WIIEDEQSLK SGLPHKYGVN
     DIPLILQDMR LNNQGLQLFQ PNQTALFGNR LFVNGQEAPY VNVPRGWVRL RLVNASLSRH
     YELRLDDERE MRLIASDQGF LPQAKVLKSI VLAPSERSEL LIDLNEGESV RLIAGEKRDF
     LHVFTSLFAD ENELVDNTVL ELRPEGLASV FSKQAEPQFN TDAVANLSNK VVQERQFHFD
     VNTGMVNDKH FDPKRVTNAK LNTTERWTLT ANGIMGFRIQ GAKFLIESIN DTSVEQSEIA
     WKDSVLINGK VQILVKFEHM SSNNHPFLFG SANLMLADKG CIRLLVVQ