ID Q2SJZ2_HAHCH Unreviewed; 964 AA.
AC Q2SJZ2;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=Protease 3 {ECO:0000256|ARBA:ARBA00017565};
DE EC=3.4.24.55 {ECO:0000256|ARBA:ARBA00012449};
DE AltName: Full=Pitrilysin {ECO:0000256|ARBA:ARBA00033450};
DE AltName: Full=Protease III {ECO:0000256|ARBA:ARBA00031184};
DE AltName: Full=Protease pi {ECO:0000256|ARBA:ARBA00029597};
GN OrderedLocusNames=HCH_02204 {ECO:0000313|EMBL:ABC29032.1};
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC29032.1, ECO:0000313|Proteomes:UP000000238};
RN [1] {ECO:0000313|EMBL:ABC29032.1, ECO:0000313|Proteomes:UP000000238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC29032.1,
RC ECO:0000313|Proteomes:UP000000238};
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
CC -!- FUNCTION: Endopeptidase that degrades small peptides of less than 7
CC kDa, such as glucagon and insulin. {ECO:0000256|ARBA:ARBA00002184}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CP000155; ABC29032.1; -; Genomic_DNA.
DR RefSeq; WP_011396101.1; NC_007645.1.
DR AlphaFoldDB; Q2SJZ2; -.
DR STRING; 349521.HCH_02204; -.
DR KEGG; hch:HCH_02204; -.
DR eggNOG; COG1025; Bacteria.
DR HOGENOM; CLU_004639_1_1_6; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000000238; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR032632; Peptidase_M16_M.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000238};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..964
FT /note="Protease 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004215798"
FT DOMAIN 51..187
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 213..388
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 404..665
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 679..842
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 964 AA; 110746 MW; 0B29B63FD3C467CA CRC64;
MFFRCITHVI YAAFALTLSV NAYAEEINPL LPKDCEQSKQ YSYLQLDNGL KVLTISDSSL
NKARIALEAS VGTQQDPQDI LGMAHFLEHM LFLGSEKYPD ADGLQTYLAQ HGGSTNATTD
YNATNYHFDV EPKHLEGALD LFADAMSAPR LDSTYVGRER NAIQAEYQYR KDMVYWRLTD
AASEAFATNH PITRFGMGNA KSFEAFNDQE LANRVRAWWT THYSAEKMSL VISAPQSNEV
LESLVKEKFK RLPVRQAAPR ANQEPLRLNR IPSLVKTKFN DLERYMILYF PISDIREEYK
AAPEEFIRYL LEQQVPQTLS SNLRGYSYAK GVSVRFNTDD PGASRIEVYV NLHYKGGEQY
WDVIRRLMAY VDILKKAPLE EWRFNEFQKT RGLQWCYFDD LSIANTAHNL NLYGPSYALA
KGYVAEEFNP ALYQKILEAI RPDNMMAIVT HPDFVLSRES KWFSTPYSVS MLSPSEQKHY
LPKESYYMAL PPANPFLPKG KVQIAGGDIA ATPELLNTHQ NIKAWYGKNT EAGSPLAYYF
VSLRSPEMDK DQRSAALTQL FWSLLRKKFE HQMLIAEEVN TTLDIERQKN GIALHFHGYP
ESIELLLSQI LEEIKTFRVK ERRYEGYRYG WMEFLNKYTE ETHPLTVAQE TADNILYSPS
YSRSDLGKGM QGASYSRMIN LLEDFKNSLH VTSLAYGNIE QAQAEAWNKM VADAIVNKKS
TPRIKEYVTR IPKGVTRLFE ESIFTDSVSL VYVQGSSASY EERAHFKLLE KMLSESFFKE
LRTEKQLGYV VHATSNNYLH IPGMKFKMQS PVSGPDKLEL ETLSFIKGFF DILKDIQEKD
FSVFKNTLVA ELNADKELEN KAYGYWKEIK NGSLHFDASK RMADAVESIS RDNFINWYGQ
RFTSSESRLL SILVEGDAHS IDTHWKSQVS STKLRSLEKF QNSNQKWVLE TPQSESVELM
LSKQ
//