ID   A0A0B2C234_9SPHN        Unreviewed;       524 AA.
AC   A0A0B2C234;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Protease {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PK98_07620 {ECO:0000313|EMBL:KHL26317.1};
OS   Croceibacterium mercuriale.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceibacterium.
OX   NCBI_TaxID=1572751 {ECO:0000313|EMBL:KHL26317.1, ECO:0000313|Proteomes:UP000030988};
RN   [1] {ECO:0000313|EMBL:KHL26317.1, ECO:0000313|Proteomes:UP000030988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Coronado {ECO:0000313|EMBL:KHL26317.1,
RC   ECO:0000313|Proteomes:UP000030988};
RA   Coil D.A., Eisen J.A.;
RT   "Draft genome sequence of Kirrobacter mercurialis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KHL26317.1}.
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DR   EMBL; JTDN01000001; KHL26317.1; -; Genomic_DNA.
DR   RefSeq; WP_039095481.1; NZ_JTDN01000001.1.
DR   AlphaFoldDB; A0A0B2C234; -.
DR   STRING; 1572751.PK98_07620; -.
DR   OrthoDB; 9766361at2; -.
DR   Proteomes; UP000030988; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR43019:SF23; PROTEASE DO-LIKE 5, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030988};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..524
FT                   /note="Protease"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002067929"
FT   TRANSMEM        302..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        337..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   524 AA;  54531 MW;  B147BD3141F088F7 CRC64;
     MVASLFRLLL SAVLLALLVA PSPARADPAD IDAAARGVVR VVIIDRRGGQ VTPLSHGSGF
     AIGTERVVTN AHVVRQAVAD PSLAIGIVPS DGGDAIYARL VTISDRNDLA LLATTAPMAL
     PPLTVSGNPA VDAGSVVAVG YPMNVDRAQG LSAGDLFRAV PPVKSAGFLS GRRPSRDFDT
     LLHTAPIARG NSGGPLLDEC GRVVGVNSFG TESGSADAEF FFAVSTRELL PFLTANGVVP
     RVNSSPCRSL ADLEAAEAGR AEREAQDAAR AAEADAASTA RRQADARRAI EFEIIAEREN
     GMAATFLLLI AGFAAALYGM FLHEFPRENE TATRPRIAFA VAALALLGAG GAWAARPGFA
     QVEGRLADSL LAQRTAEAGG SDAGDNPAGS YTCVLDESRS RVVGDAAGDV AIRWAADGCV
     NGRTQYARTG GDWTRILVPE EEAAATVNRF DPATGEYRVD RYLLGREARE AARAARGGYQ
     VPQCGGGGAA AIQLAQRQQA ILAVLPPAPN ERLVYRCTKN DAGR
//