ID   HTRA_SYNY3              Reviewed;         452 AA.
AC   P73354;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Putative serine protease HtrA;
GN   Name=htrA; OrderedLocusNames=slr1204;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   SUBCELLULAR LOCATION IN OUTER MEMBRANE.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=14990684; DOI=10.1074/mcp.m300137-mcp200;
RA   Huang F., Hedman E., Funk C., Kieselbach T., Schroder W.P., Norling B.;
RT   "Isolation of outer membrane of Synechocystis sp. PCC 6803 and its
RT   proteomic characterization.";
RL   Mol. Cell. Proteomics 3:586-595(2004).
RN   [3]
RP   FUNCTION IN PHOTOPROTECTION, PROTECTION AGAINST HEAT STRESS, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=16912048; DOI=10.1074/jbc.m601064200;
RA   Barker M., de Vries R., Nield J., Komenda J., Nixon P.J.;
RT   "The deg proteases protect Synechocystis sp. PCC 6803 during heat and light
RT   stresses but are not essential for removal of damaged D1 protein during the
RT   photosystem two repair cycle.";
RL   J. Biol. Chem. 281:30347-30355(2006).
RN   [4]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=17208194; DOI=10.1016/j.bbabio.2006.11.016;
RA   Cheregi O., Sicora C., Kos P.B., Barker M., Nixon P.J., Vass I.;
RT   "The role of the FtsH and Deg proteases in the repair of UV-B radiation-
RT   damaged Photosystem II in the cyanobacterium Synechocystis PCC 6803.";
RL   Biochim. Biophys. Acta 1767:820-828(2007).
CC   -!- FUNCTION: A putative protease, its function overlaps that of the
CC       related putative proteases HhoA and HhoB.
CC       {ECO:0000269|PubMed:16912048}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000269|PubMed:14990684}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:14990684}.
CC   -!- INDUCTION: No induction by UV-B light. {ECO:0000269|PubMed:17208194}.
CC   -!- DISRUPTION PHENOTYPE: No effect in a single knockout, but growth is
CC       inhibited at high light (120 umol photons/m(2)/s) or at elevated
CC       temperature in a triple protease knockout mutant (hhoA, hhoB and htrA).
CC       Triple mutants are not phototactic. No effect on the PSII repair cycle,
CC       even in the triple protease knockout strain.
CC       {ECO:0000269|PubMed:16912048, ECO:0000269|PubMed:17208194}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA17385.1; -; Genomic_DNA.
DR   PIR; S77538; S77538.
DR   AlphaFoldDB; P73354; -.
DR   SMR; P73354; -.
DR   IntAct; P73354; 22.
DR   STRING; 1148.1652463; -.
DR   MEROPS; S01.482; -.
DR   PaxDb; P73354; -.
DR   EnsemblBacteria; BAA17385; BAA17385; BAA17385.
DR   KEGG; syn:slr1204; -.
DR   eggNOG; COG0265; Bacteria.
DR   InParanoid; P73354; -.
DR   OMA; DTRHFDY; -.
DR   PhylomeDB; P73354; -.
DR   BRENDA; 3.4.21.107; 6192.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   Pfam; PF13180; PDZ_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..452
FT                   /note="Putative serine protease HtrA"
FT                   /id="PRO_0000400422"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          352..434
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
SQ   SEQUENCE   452 AA;  47656 MW;  AED4AFB1AC472361 CRC64;
     MSAQAVFPIA PHRADFFPRF VLSNSSANKC HQAMKDVSLH SPKQTPSKIS LAYLGLVLVG
     MGIGAGGTFV LTNPQWADHL TNNSVISPLV TNQSIAPANE SLATNLQSRL SPREPSNFVV
     DVVESTGPAV VRINAQKTVK SQVPQAFNDP FLQRFFGSQM PPMPNERVQR GTGSGFIVSN
     DGKIFTNAHV VDGADEVTVT LKDGRSFPGR VMGSDPSTDV AVVKIEAGDL PTVALGDSDH
     LQVGEWAIAI GNPLGLDNTV TTGILSATGR RSADIGVPDK RVEFIQTDAA INPGNSGGPL
     LNADGQVIGM NTAIIQNAQG IGFAIPINKA QEIAQQLIAT GKVEHAYLGI QMVTMTPELQ
     SQIRQETGMN IPVDKGVVIM QVMPNSPAAI AKLEQGDVLQ SLQGQPVENA EQVQSLVGKL
     AVGDEVELGI LRNGQQQNLT VTIGALPSAP PQ