ID   FTSP_AGGAN              Reviewed;         470 AA.
AC   C6AK71;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-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=NT05HA_0118;
OS   Aggregatibacter aphrophilus (strain NJ8700) (Haemophilus aphrophilus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=634176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJ8700;
RX   PubMed=19447908; DOI=10.1128/jb.00447-09;
RA   Di Bonaventura M.P., DeSalle R., Pop M., Nagarajan N., Figurski D.H.,
RA   Fine D.H., Kaplan J.B., Planet P.J.;
RT   "Complete genome sequence of Aggregatibacter (Haemophilus) aphrophilus
RT   NJ8700.";
RL   J. Bacteriol. 191:4693-4694(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; CP001607; ACS96560.1; -; Genomic_DNA.
DR   RefSeq; WP_005704339.1; NZ_CP009230.1.
DR   AlphaFoldDB; C6AK71; -.
DR   SMR; C6AK71; -.
DR   PRIDE; C6AK71; -.
DR   GeneID; 49635293; -.
DR   KEGG; aap:NT05HA_0118; -.
DR   PATRIC; fig|634176.19.peg.111; -.
DR   HOGENOM; CLU_009100_2_4_6; -.
DR   OMA; GMWIIED; -.
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; Signal.
FT   SIGNAL          1..29
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00915"
FT   CHAIN           30..470
FT                   /note="Cell division protein FtsP"
FT                   /id="PRO_0000416004"
SQ   SEQUENCE   470 AA;  52286 MW;  DA9142BE59B10CAF CRC64;
     MKNCSRRQLL KTTLFSTALF SVPAPLLAAT RPTLTIPPLF ETRRGKPIFL NLQNTQASLL
     PGKRTEVWGF NGVYLGPTIK IKKDDFAKLN WKNNLPQFVA MNIQGLQASG ELIGGIAKNL
     QKDETWAPII PITQAPSTCW YHACTLANSA YQTYRGLLGL WMIEDKESTK LGLPQKYGVD
     DIPLILQDMQ LNTEGTQLFQ QHQGRFIGER LFVNGQEAPY LTVPRGLVRL RVLNASLSRT
     YELRFDDERE FTLIAQDLGF LPQGQKRNVV MLAPSERVEI LVDLNDGENV SLITGTKRGI
     LDNISHFFGS DGELIDNTIL ELRPEGLAGA FEKKEQTWQF NTDAPSLLST KVQQERAFHI
     DVGNATINKN RLDPRRLDVS AKLGSVERWT LSASSPVGFA IRGAKFIVES VNGKALEASE
     IGWKDSVLIN GKVSILVKFE NTSSNNYPFT FGASDLMLAD KGCIGLMLVQ