HLY_HALMT
ID HLY_HALMT Reviewed; 519 AA.
AC I3R794; P71402;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Halolysin;
DE EC=3.4.21.-;
DE AltName: Full=Halophilic serine protease;
DE Flags: Precursor;
GN Name=hly; OrderedLocusNames=HFX_2419; ORFNames=C439_13889;
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 117-136, FUNCTION,
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-432 AND CYS-468.
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=8645734; DOI=10.1016/0167-4838(96)00016-7;
RA Kamekura M., Seno Y., Dyall-Smith M.;
RT "Halolysin R4, a serine proteinase from the halophilic archaeon Haloferax
RT mediterranei; gene cloning, expression and structural studies.";
RL Biochim. Biophys. Acta 1294:159-167(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=22843593; DOI=10.1128/jb.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- FUNCTION: Probable secreted halophilic serine protease showing
CC proteolytic activity toward the protease general substrate azocasein.
CC {ECO:0000269|PubMed:8645734}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D64073; BAA10958.1; -; Genomic_DNA.
DR EMBL; CP001868; AFK20104.1; -; Genomic_DNA.
DR EMBL; AOLO01000011; ELZ99650.1; -; Genomic_DNA.
DR PIR; S71451; S71451.
DR RefSeq; WP_004059827.1; NZ_CP039139.1.
DR AlphaFoldDB; I3R794; -.
DR SMR; I3R794; -.
DR STRING; 523841.HFX_2419; -.
DR MEROPS; S08.102; -.
DR EnsemblBacteria; AFK20104; AFK20104; HFX_2419.
DR EnsemblBacteria; ELZ99650; ELZ99650; C439_13889.
DR GeneID; 40157691; -.
DR KEGG; hme:HFX_2419; -.
DR eggNOG; arCOG00702; Archaea.
DR HOGENOM; CLU_011263_15_0_2; -.
DR OMA; WSADQGA; -.
DR OrthoDB; 20800at2157; -.
DR Proteomes; UP000006469; Chromosome.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07484; Peptidases_S8_Thermitase_like; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR034084; Thermitase-like_dom.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Protease; Secreted; Serine protease;
KW Signal; Zymogen.
FT SIGNAL 1..27
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT PROPEP 28..116
FT /evidence="ECO:0000269|PubMed:8645734"
FT /id="PRO_0000428908"
FT CHAIN 117..519
FT /note="Halolysin"
FT /id="PRO_0000428909"
FT DOMAIN 127..400
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 386..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 347
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT MUTAGEN 432
FT /note="C->S: Decreases stability in hypotonic solutions."
FT /evidence="ECO:0000269|PubMed:8645734"
FT MUTAGEN 468
FT /note="C->S: Decreases stability in hypotonic solutions."
FT /evidence="ECO:0000269|PubMed:8645734"
FT CONFLICT 257
FT /note="G -> V (in Ref. 1; BAA10958)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="D -> G (in Ref. 1; BAA10958)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 53516 MW; 039E41F8AFD37ADD CRC64;
MAGTPNFDRR SFLRLAAAAG LTGMAGVTSA TPGRSPGPKK DEILVGVTST ADSPRKAVAD
AVPGNAEIVH ENETLSYAAV KFPSKAPKQA RENFISAITK RDEVKYAEKN ATHEALYTAN
DPKYGSQYAP QQVNADSAWD TTLGSSSVKI AVVDQGVKYD HPDLSSQFGS NKGRDFVDND
GDPYPDLLSD EYHGTHVAGI AAGTTDNNEG IGGISNSTLL SGRALSESGS GSTSDIADAI
EWAADQGADV INLSLGGGGY SSTMKNAVSY ATQQGSLVVA AAGNDGRQSV SYPAAYSECV
AVSALDPDET LASYSNYGSE IDLAAPGTNV LSCWTTSTEY NEISGTSMAT PVVSGVAGLA
LAVHNLSPAD LRNHLKNTAV DIGLSSTKQG SGRVDAANAV TTDPGDGGGG GGGGSKETTY
DGTLSSSSDS NCVSHSWNYS SPSQVVIDLS GPSSADFDLY ATEGSGTCPT TRSYDYRSWS
YDSTEQIVID NPDTSADLGI LVDSYSGSGS YTVTITEKE
