ID   Y4QF_SINFN              Reviewed;         754 AA.
AC   P55627;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Uncharacterized peptidase y4qF;
DE            EC=3.4.21.-;
GN   OrderedLocusNames=NGR_a01920; ORFNames=y4qF;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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DR   EMBL; U00090; AAB91830.1; -; Genomic_DNA.
DR   RefSeq; NP_444033.1; NC_000914.2.
DR   RefSeq; WP_010875226.1; NC_000914.2.
DR   AlphaFoldDB; P55627; -.
DR   SMR; P55627; -.
DR   ESTHER; rhisn-y4qf; S9N_PREPL_Peptidase_S9.
DR   EnsemblBacteria; AAB91830; AAB91830; NGR_a01920.
DR   KEGG; rhi:NGR_a01920; -.
DR   PATRIC; fig|394.7.peg.191; -.
DR   eggNOG; COG1770; Bacteria.
DR   HOGENOM; CLU_011290_0_1_5; -.
DR   OMA; HIANEYR; -.
DR   OrthoDB; 154149at2; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR023302; Pept_S9A_N.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002470; Peptidase_S9A.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Plasmid; Protease; Reference proteome; Serine protease.
FT   CHAIN           1..754
FT                   /note="Uncharacterized peptidase y4qF"
FT                   /id="PRO_0000122406"
FT   REGION          733..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        585
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        707
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   754 AA;  84714 MW;  B5CD67884FA74D23 CRC64;
     MGGLSAMQRR IDLLVEGGDE YDACSHFRSV VMWDKSLRPP LPRAEPRIRV LHDDVTVDRY
     GWLRDRENPD VRAYLEAENS YAEQATAHLR RLKTELIAEI EGRQPCEGAT PPFQVGPFDY
     FQGHERGLPH PVWWRRPVTG GSAELVLDPN AIPGADVFYW LGVFEPSDDG RYLAFSVDLI
     GAERYELRVR DMSDGRDVWR DAGSVGQVVW AADNHTLFFT RERPDRRQHH QIVRLNVGRG
     NSEVVFEEAN ERLAVLVRRS QSGAWLFLDV LTTSDMSSYV QRGAAEVWCL PADEPGGQWR
     RIVMRELGHQ IYAEHWYDRF LFRVDDAGPY WRLVSAPIDD PSPSRWEEVV PHRAGVTIDE
     IHVLEQHLVL LEREGLRPRL ISRNRSGRVG AVIVPDEPSC TIRVGLSAGG CYSAARHPFR
     SSKLTYSVSS FVTPDTFIEH DFANDRSVVL CEARVPGYDA TQYLATVVMA EAEDGVQVPI
     SLVARRDRTS PGPVLLSVYG CYGIPRLPSF LAWPSSMTAR LSLLDREVAF GIVHVRGGGE
     LGRPWHDAAT RDQKRITHTD LISATEGLIE RGFATRDGVV IEGKSGGGGT VLATAVFRPN
     LFRAVVAEVP LADIIDTQLD STMPYTLKET AEYGDPQDAY EYRYLRSYDP YYNLSPERSL
     PPTYVDAALD DGQVIYYQPA RYVAQRRSCA TDRDPDLVFR IRMVGGHSGP SHGPGIAEQA
     AFRMAWVLDQ LRSHAPPPSR KARSAARRST DPVR