FTSP_RAHSY
ID FTSP_RAHSY Reviewed; 471 AA.
AC E8XXT6;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
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=Rahaq_0641;
OS Rahnella sp. (strain Y9602).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Rahnella.
OX NCBI_TaxID=2703885;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y9602;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Pagani I., Sobecky P.A., Martinez R.J.,
RA Woyke T.;
RT "Complete sequence of chromosome of Rahnella sp. Y9602.";
RL Submitted (JAN-2011) 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; CP002505; ADW72268.1; -; Genomic_DNA.
DR RefSeq; WP_013573973.1; NC_015061.1.
DR AlphaFoldDB; E8XXT6; -.
DR SMR; E8XXT6; -.
DR STRING; 741091.Rahaq_0641; -.
DR EnsemblBacteria; ADW72268; ADW72268; Rahaq_0641.
DR KEGG; rah:Rahaq_0641; -.
DR eggNOG; COG2132; Bacteria.
DR HOGENOM; CLU_009100_2_4_6; -.
DR OMA; GMWIIED; -.
DR OrthoDB; 971126at2; -.
DR Proteomes; UP000007257; 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 InterPro; IPR019546; TAT_signal_bac_arc.
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 Pfam; PF10518; TAT_signal; 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; Signal.
FT SIGNAL 1..27
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00915"
FT CHAIN 28..471
FT /note="Cell division protein FtsP"
FT /id="PRO_5000703684"
FT DOMAIN 229..288
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00915"
SQ SEQUENCE 471 AA; 51081 MW; FB695D1521A33DDE CRC64;
MSLSRRSFLQ ASGVALAAGA LPLKAEASGS QPALPVPPLL ESRRGQPLFL TLQAAHWSFL
GGAKAPVWGI NGMYLGPTVK VHSGDDVKLI YSNRLAEPVS MTVSGLLEPG TLTGGAARLM
QPGVDWSPVL PIRQAAATCW YHANTPNRMA PHVYNGLAGM WIVEDEVSKN LPLPNHYGVD
DFPIIIQDKR LDGFGVPQYD TPASGGFFGD TMLVNGVQSP YVEVSRGWVR LRLLNASNAR
RYELSMTDNR AFHVVASDLG FLPAPMTVKR LSLGPGERRE VLVDMSQGEE VSITAGEAAG
VMDRLRGLFE PSSILVSTIV LTLKPTGLLP LVTDNLPMRL LADQILSGNV VRTRDLRLGD
SEPGINGAMW DINRIDLTAQ QGTWERWTVH ADMPQTFHAE GVSFLVKSVN GAAPLVEDAG
FKDTVWVDGD VELLVYFNQP SYEHFPFVYR SGALELADRG SAGNMLVQPS M