ID   FTSP_HISS2              Reviewed;         467 AA.
AC   B0UVZ0;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=HSM_1771;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) 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: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; CP000947; ACA31553.1; -; Genomic_DNA.
DR   RefSeq; WP_012340876.1; NC_010519.1.
DR   AlphaFoldDB; B0UVZ0; -.
DR   SMR; B0UVZ0; -.
DR   STRING; 228400.HSM_1771; -.
DR   EnsemblBacteria; ACA31553; ACA31553; HSM_1771.
DR   KEGG; hsm:HSM_1771; -.
DR   HOGENOM; CLU_009100_2_4_6; -.
DR   OMA; GMWIIED; -.
DR   OrthoDB; 971126at2; -.
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   PANTHER; PTHR11709; PTHR11709; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   SUPFAM; SSF49503; SSF49503; 3.
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..467
FT                   /note="Cell division protein FtsP"
FT                   /id="PRO_5000311171"
SQ   SEQUENCE   467 AA;  52306 MW;  79394041263BBC1D CRC64;
     MRSLTRRDFL KSGILASSLS CIPQSVMAAS RLPLFIPPLL EAKRGRPIFL TMQAAQTSFI
     EKKLTEVWGF NGHHLGPTVR VEQGDFVKLN YRNNLTQAVA MNIQGLQAHS ELIGGIGRVL
     KAGEGWAPIL PITQPASTCF YHACTLANSA YQTYRGLVGM WIINDKDTHQ SKLPKKYGVD
     DIPLILQDVL LNSKGEQVFQ NQPHFLGERL LVNGVEAPYL NVPKGLVRLR LLNASLSRSY
     DLTFDDERAF FLIAREQGYL PQTKIVKKVS LAPSERVELL VDLSEGGNVT LITGSKRNLL
     NKIGTIFSSD MLVDNVIVEL RTEGVKSVFY NPSHWQFHTD APSLLAKKNM KTREFYFDVS
     NATINQQRFE PNRIDISTKR GQIERWILSS SRPVGFKIQG ARFVMKSIND QPVEQSDIAW
     KDSLWIDGKV EILVQFNHAS STKFPFIFGS SDLVLADQGC LGSIVVQ