HHOB_SYNY3
ID HHOB_SYNY3 Reviewed; 416 AA.
AC P73940;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Putative serine protease HhoB;
DE Flags: Precursor;
GN Name=hhoB; OrderedLocusNames=sll1427;
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 FUNCTION IN PHOTOPROTECTION, PROTECTION AGAINST HEAT STRESS, AND DISRUPTION
RP PHENOTYPE.
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 [3]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
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 HtrA and HhoA.
CC {ECO:0000269|PubMed:16912048}.
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; BAA18006.1; -; Genomic_DNA.
DR PIR; S75445; S75445.
DR AlphaFoldDB; P73940; -.
DR SMR; P73940; -.
DR IntAct; P73940; 15.
DR STRING; 1148.1653090; -.
DR MEROPS; S01.482; -.
DR PaxDb; P73940; -.
DR EnsemblBacteria; BAA18006; BAA18006; BAA18006.
DR KEGG; syn:sll1427; -.
DR eggNOG; COG0265; Bacteria.
DR InParanoid; P73940; -.
DR OMA; THGWVLE; -.
DR PhylomeDB; P73940; -.
DR BRENDA; 3.4.21.107; 6192.
DR Proteomes; UP000001425; Chromosome.
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 InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
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 Hydrolase; Protease; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..416
FT /note="Putative serine protease HhoB"
FT /id="PRO_0000400423"
FT DOMAIN 320..398
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 35..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 43196 MW; DD32BB997CC6B25B CRC64;
MAIHLKASHL GVAVLLLLFG GAIGAAGGGY LLSSGQNHSS PDSPVNTSPQ SLTPAPVESN
YRSALPLTLP RSAQDDQELN FIARAVQKIG PAVVRIDSER TAVSQGGPMG DQPFFRRFFG
EEMPPNPDPR EQGTGSGFIL SSDGEVLTNA HVVEGASTVK VTLKDGSVLE GKVMGIDTMT
DVAVVKVEAE NLPVVEIGQS DRLQPGEWAI AIGNPLGLDN TVTVGIISAL GRSSSEVGVP
DKRVRFIQTD AAINPGNSGG PLLNAKGEVI GVNTAIRADA QGLGFAIPIQ TAQNVAENLF
TKGKMEHPYL GIHMVTLTPE MTKQLRTSGE LPAGVTADTG VLIIQVSPGS PAAQAGLAPG
DIILEVGGMG VKTATDVQER VEVSQIGEPL AIAVKRGQKP QMMAVRPGPF PEDLGQ