ID M4NJ41_9GAMM Unreviewed; 434 AA.
AC M4NJ41;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Subtilisin-like serine protease {ECO:0000313|EMBL:AGG87821.1};
DE Flags: Precursor;
GN ORFNames=R2APBS1_0653 {ECO:0000313|EMBL:AGG87821.1};
OS Rhodanobacter denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=666685 {ECO:0000313|EMBL:AGG87821.1, ECO:0000313|Proteomes:UP000011859};
RN [1] {ECO:0000313|EMBL:AGG87821.1, ECO:0000313|Proteomes:UP000011859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2APBS1 {ECO:0000313|EMBL:AGG87821.1,
RC ECO:0000313|Proteomes:UP000011859};
RG US DOE Joint Genome Institute;
RA Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Munk A.C.C., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Peters L., Pitluck S., Woyke T., Prakash O., Elkins J., Brown S.,
RA Palumbo A., Hemme C., Zhou J., Watson D., Jardine P., Kostka J., Green S.;
RT "Complete genome of Rhodanobacter sp. 2APBS1.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CP003470; AGG87821.1; -; Genomic_DNA.
DR RefSeq; WP_015446853.1; NZ_CP088918.1.
DR AlphaFoldDB; M4NJ41; -.
DR STRING; 666685.R2APBS1_0653; -.
DR KEGG; rhd:R2APBS1_0653; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_051649_0_0_6; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000011859; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..434
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004056243"
FT DOMAIN 184..408
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 192
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 375
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 434 AA; 45198 MW; C006B0258C4A0120 CRC64;
MKHGAIVFAA AMALSACAHL RPAAPADDPA DPHRSSVASA SAMDSRRDIV LAVANPLAPP
ATHAGSSVLG YVPSANYGVG QRAASTLAAL KRTYGWQEVT GWPVKALDLY CIVLTPAPGM
PRAALLKALA ADARVRLAQP LQDYSVYADP PRQDAHHYND PYADLQRGFV ETDAALAHNL
SQGAEVDVAI VDTGVDLTHP DLRGRIRDTR NLVDADRAAF DRDNHGTEVA GVIAADADNH
QGIVGMAPKA RLSIYKACWY PPSPGAGARC NTFTLAKALA AVIDTDTRII NLSLGGPADP
LLDQLLARLL EQGRIVITAM PPDGNAAGFP DRAPGVIVVR SSNASRAPPG VLSAPGNDIL
TTQPDGGYDF TSGSSMAAAH VSGIAALLLA MAPGLDARSM HDLLLQSSRL SDGTLQVNAA
SAVARLRNEE KAAP
//
