HHOA_SYNY3
ID HHOA_SYNY3 Reviewed; 394 AA.
AC P72780;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Putative serine protease HhoA;
DE Flags: Precursor;
GN Name=hhoA; OrderedLocusNames=sll1679;
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.
RX PubMed=10998049; DOI=10.1046/j.1432-1327.2000.01642.x;
RA Fulda S., Huang F., Nilsson F., Hagemann M., Norling B.;
RT "Proteomics of Synechocystis sp. strain PCC 6803. Identification of
RT periplasmic proteins in cells grown at low and high salt concentrations.";
RL Eur. J. Biochem. 267:5900-5907(2000).
RN [3]
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 [4]
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 HhoB and HtrA.
CC {ECO:0000269|PubMed:16912048}.
CC -!- INTERACTION:
CC P72780; P72780: hhoA; NbExp=2; IntAct=EBI-1610232, EBI-1610232;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- INDUCTION: Slight induction by UV-B light.
CC {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; BAA16795.1; -; Genomic_DNA.
DR PIR; S74643; S74643.
DR PDB; 5B6L; X-ray; 2.80 A; A=56-394.
DR PDB; 5GND; X-ray; 2.50 A; A=56-394.
DR PDB; 5T63; X-ray; 2.50 A; A=35-394.
DR PDB; 5T69; X-ray; 2.10 A; A=35-394.
DR PDBsum; 5B6L; -.
DR PDBsum; 5GND; -.
DR PDBsum; 5T63; -.
DR PDBsum; 5T69; -.
DR AlphaFoldDB; P72780; -.
DR SMR; P72780; -.
DR IntAct; P72780; 13.
DR STRING; 1148.1651868; -.
DR MEROPS; S01.482; -.
DR PaxDb; P72780; -.
DR EnsemblBacteria; BAA16795; BAA16795; BAA16795.
DR KEGG; syn:sll1679; -.
DR eggNOG; COG0265; Bacteria.
DR InParanoid; P72780; -.
DR OMA; IIGINRQ; -.
DR PhylomeDB; P72780; -.
DR BRENDA; 3.4.21.107; 6192.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; HDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 3D-structure; Hydrolase; Periplasm; Protease; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..394
FT /note="Putative serine protease HhoA"
FT /id="PRO_0000400424"
FT DOMAIN 293..377
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:5T69"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:5T69"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:5T69"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 145..154
FT /evidence="ECO:0007829|PDB:5T69"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:5T69"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:5T69"
FT TURN 234..238
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:5T69"
FT HELIX 268..279
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:5T69"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 316..325
FT /evidence="ECO:0007829|PDB:5T69"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 341..349
FT /evidence="ECO:0007829|PDB:5T69"
FT HELIX 353..363
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 368..374
FT /evidence="ECO:0007829|PDB:5T69"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:5T69"
SQ SEQUENCE 394 AA; 41336 MW; AD59D94811B8F57B CRC64;
MKYPTWLRRI GGYLLAFAVG TAFGIANLPH AVAAADDLPP APVITAQASV PLTSESFVAA
AVSRSGPAVV RIDTETVVTR RTDPILDDPF FQEFFGRSFP VPPRERRIAG QGSGFIIDNS
GIILTNAHVV DGASKVVVTL RDGRTFDGQV RGTDEVTDLA VVKIEPQGSA LPVAPLGTSS
NLQVGDWAIA VGNPVGLDNT VTLGIISTLG RSAAQAGIPD KRVEFIQTDA AINPGNSGGP
LLNARGEVIG INTAIRADAT GIGFAIPIDQ AKAIQNTLAA GGTVPHPYIG VQMMNITVDQ
AQQNNRNPNS PFIIPEVDGI LVMRVLPGTP AERAGIRRGD VIVAVDGTPI SDGARLQRIV
EQAGLNKALK LDLLRGDRRL SLTVQTAQLR NPTS
