ID   FTSP_SALTY              Reviewed;         470 AA.
AC   P0A1C5; P40799;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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}; Synonyms=sufI;
GN   OrderedLocusNames=STM3172;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RA   Cong J., Schmid M.B.;
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA56679.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U09309; AAA56679.1; ALT_FRAME; Unassigned_DNA.
DR   EMBL; AE006468; AAL22046.1; -; Genomic_DNA.
DR   RefSeq; NP_462087.1; NC_003197.2.
DR   RefSeq; WP_000010658.1; NC_003197.2.
DR   AlphaFoldDB; P0A1C5; -.
DR   SMR; P0A1C5; -.
DR   STRING; 99287.STM3172; -.
DR   PaxDb; P0A1C5; -.
DR   EnsemblBacteria; AAL22046; AAL22046; STM3172.
DR   GeneID; 1254695; -.
DR   KEGG; stm:STM3172; -.
DR   PATRIC; fig|99287.12.peg.3363; -.
DR   HOGENOM; CLU_009100_2_4_6; -.
DR   OMA; GMWIIED; -.
DR   PhylomeDB; P0A1C5; -.
DR   BioCyc; SENT99287:STM3172-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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   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; Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00915"
FT   CHAIN           28..470
FT                   /note="Cell division protein FtsP"
FT                   /id="PRO_0000002996"
FT   DOMAIN          222..287
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00915"
SQ   SEQUENCE   470 AA;  51858 MW;  61E84D4D42B025FB CRC64;
     MSFSRRQFLQ ASGIALCAGA IPLRANAAGQ QQPLPVPPLL ESRRGQPLFM TLQRAHWSFT
     QGTRAPVWGV NGRYLGPTIR VWKGDDVKLI YSNRLAENVS MTVAGLLVPG PLMGGPARMM
     SPNADWAPVL PIRQSAATLW YHANTPNRTA QQVYNGLAGM WLVEDDISKT LPIPNHYGVD
     DFPVIIQDKR LDNFGTPEYS EPGSGGFVGD TLLVNGAQSP YVEVSRGWVR LRLLNASNSR
     RYQLQMSDGR ALHVISGDQG FLPAPVSVKQ LSLAPGERRE ILVDMTNGDE VSITCGEAAS
     IVDRIRGFFE PSSILVSTLV LTLRPTGLLP LVTDNLPMRL LPTEIMSGAP VRSRDISLGD
     DPGINGQLWD VNRIDITAQQ GTWERWTVRA DMPQSFHIEG VSFLIRNVNG AMPFPEDRGW
     KDTVWVDGQV ELLVYYGQPS WPHFPFYFNS QTLEMADRGS IGQMLVNPAS