FTSP_HAEI8
ID FTSP_HAEI8 Reviewed; 469 AA.
AC Q4QMG3;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=NTHI0890;
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP;
RX PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S. Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX87784.1; -; Genomic_DNA.
DR RefSeq; WP_005689021.1; NC_007146.2.
DR AlphaFoldDB; Q4QMG3; -.
DR SMR; Q4QMG3; -.
DR PRIDE; Q4QMG3; -.
DR EnsemblBacteria; AAX87784; AAX87784; NTHI0890.
DR KEGG; hit:NTHI0890; -.
DR HOGENOM; CLU_009100_2_4_6; -.
DR OMA; GMWIIED; -.
DR OrthoDB; 971126at2; -.
DR Proteomes; UP000002525; 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; IPR001117; Cu-oxidase.
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; PF00394; Cu-oxidase; 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..29
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00915"
FT CHAIN 30..469
FT /note="Cell division protein FtsP"
FT /id="PRO_0000416009"
FT DOMAIN 228..286
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00915"
SQ SEQUENCE 469 AA; 52118 MW; CB3C93B65E518DB3 CRC64;
MPRLSRRQLL KTAAISTALS TVPAPLLAAS REKLVVPPLI EVRRGRPIVL TMQETNYPLD
GSHNVTVWGF NGNYLGPTIK IKSGSFAKLN YHNNLPQSVA LSIQGLQASG ELFGGAARVL
KKGESWAPIV PIEQPAASCW YRSATLANSA YQTYRGLAGM WLIEDEQSLK ANLPNKYGVD
DIPLILQDME FNNDGLQLFK QNQPHFVGNR LLVNGIEAPY LDVARGWIRL RLLNASLARA
YDLRLDNDQE MLLIAQDLSF LPKAKSVKSL VLSPGERAEI LVNMNEIDNV SLISGSKRSL
YEKIKNMLFS GDELANNTVL ELRAQGQLSA FNKQPNLTFE TDAPAILQQA VAQTREFNID
VTNGLINQRR FDPRKVDVMA RKGTIERWIL NASLPVGFTI QGAKFVVESQ GEHQLQAEEL
AWKDTVWVKN KTQILVKFDQ ASSGNFPFLF GVSNLMLEDM GCLGVLMVQ