ID   STIP_ACIAD              Reviewed;         383 AA.
AC   Q6FAX7;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Cysteine protease StiP;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=stiP; OrderedLocusNames=ACIAD1960;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
RN   [2]
RP   INDUCTION.
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=20511417; DOI=10.1128/aem.01806-09;
RA   Lostroh C.P., Voyles B.A.;
RT   "Acinetobacter baylyi starvation-induced genes identified through
RT   incubation in long-term stationary phase.";
RL   Appl. Environ. Microbiol. 76:4905-4908(2010).
RN   [3]
RP   FUNCTION AS A CYSTEINE PROTEASE, GENE NAME, ACTIVITY REGULATION,
RP   AUTOCATALYTIC CLEAVAGE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=24206355; DOI=10.1139/cjm-2013-0517;
RA   Reichert B., Dornbusch A.J., Arguello J., Stanley S.E., Lang K.M.,
RA   Lostroh C.P., Daugherty M.A.;
RT   "Acinetobacter baylyi long-term stationary-phase protein StiP is a protease
RT   required for normal cell morphology and resistance to tellurite.";
RL   Can. J. Microbiol. 59:726-736(2013).
CC   -!- FUNCTION: Cysteine protease that may play a role in regulating cell
CC       morphology in response to stressful conditions which likely cause
CC       oxidative damage. Appears to catalyze its own cleavage, which probably
CC       leads to its activation. {ECO:0000269|PubMed:24206355}.
CC   -!- ACTIVITY REGULATION: Is inhibited by bromopyruvate in vitro. Activity
CC       is not affected by the presence of tellurite.
CC       {ECO:0000269|PubMed:24206355}.
CC   -!- INDUCTION: Highly induced by starvation during long-term stationary
CC       phase, while shows very low expression during exponential growth.
CC       {ECO:0000269|PubMed:20511417}.
CC   -!- PTM: Is probably processed via an autocatalytic removal of a proregion
CC       of about 100 amino acids.
CC   -!- DISRUPTION PHENOTYPE: Deletion of this gene causes hypersensitivity to
CC       tellurite, altered population dynamics during long term batch culture,
CC       and, most strikingly, dramatic alteration of normal cell morphology.
CC       {ECO:0000269|PubMed:24206355}.
CC   -!- SIMILARITY: Belongs to the cysteine protease StiP family.
CC       {ECO:0000305}.
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DR   EMBL; CR543861; CAG68786.1; -; Genomic_DNA.
DR   RefSeq; WP_004927249.1; NC_005966.1.
DR   AlphaFoldDB; Q6FAX7; -.
DR   STRING; 62977.ACIAD1960; -.
DR   EnsemblBacteria; CAG68786; CAG68786; ACIAD1960.
DR   GeneID; 45234323; -.
DR   KEGG; aci:ACIAD1960; -.
DR   eggNOG; COG1358; Bacteria.
DR   HOGENOM; CLU_032640_1_0_6; -.
DR   OMA; WTGKGVI; -.
DR   OrthoDB; 1130053at2; -.
DR   BioCyc; ASP62977:ACIAD_RS09020-MON; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:UniProtKB.
DR   GO; GO:0016540; P:protein autoprocessing; IDA:UniProtKB.
DR   InterPro; IPR028157; PELOTA_dom.
DR   InterPro; IPR011215; PRTase.
DR   Pfam; PF15608; PELOTA_1; 1.
DR   Pfam; PF11202; PRTase_1; 1.
DR   PIRSF; PIRSF020979; UCP020979; 1.
PE   1: Evidence at protein level;
KW   Autocatalytic cleavage; Hydrolase; Protease; Reference proteome;
KW   Thiol protease.
FT   PROPEP          1..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000425149"
FT   CHAIN           ?..383
FT                   /note="Cysteine protease StiP"
FT                   /id="PRO_0000425150"
SQ   SEQUENCE   383 AA;  42995 MW;  272A9462D697FD1E CRC64;
     MAIINKDKAT ELILKQGFSG SYQSEQVTFL LKRTHIEPTD TAEKERLIQS GEKHYSQMIS
     LENAPTARHL ELFEQAMQQG QQRLAQEVQQ LAQTLVVEFN EPIVLVSFVR AGVPLGVLLY
     HAIQDLGRDC VHYGISIIRD RGIDFAALET IIARHGHASI VFVDGWTGKG AIRQELQRSL
     GNDTRFIGKP LPLVVLSDIA GCAWLAASGD DWLIPSGILG STISGLISRS ICEGETLSAD
     EITAENIDQW HRCIEYHHLK EFDISQQFIQ RINQIRLKLN PQSNAVWAET QQQAQQDQSQ
     QVVHKLAQEY DIQNINRIKP SIAEATRAIL RRVPDLVLLR DADDEDTRLL RHLTQITKTP
     VQVVGDQIAP YRAITLIQKL GKG