ID U1J7K5_9GAMM Unreviewed; 911 AA.
AC U1J7K5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
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 ORFNames=PCIT_16585 {ECO:0000313|EMBL:ERG17341.1};
OS Pseudoalteromonas citrea DSM 8771.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1117314 {ECO:0000313|EMBL:ERG17341.1, ECO:0000313|Proteomes:UP000016487};
RN [1] {ECO:0000313|EMBL:ERG17341.1, ECO:0000313|Proteomes:UP000016487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8771 {ECO:0000313|Proteomes:UP000016487};
RX PubMed=22535931; DOI=10.1128/JB.00265-12;
RA Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Shi M.,
RA He H.L., Zhou B.C., Zhang Y.Z.;
RT "Genome sequences of type strains of seven species of the marine bacterium
RT Pseudoalteromonas.";
RL J. Bacteriol. 194:2746-2747(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERG17341.1}.
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; AHBZ02000177; ERG17341.1; -; Genomic_DNA.
DR AlphaFoldDB; U1J7K5; -.
DR STRING; 1117314.PCIT_16585; -.
DR eggNOG; COG1025; Bacteria.
DR Proteomes; UP000016487; Unassembled WGS sequence.
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:UP000016487};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 42..179
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 202..368
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 387..656
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 673..835
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 911 AA; 104529 MW; 00B0248BF106BA26 CRC64;
MNSSSKWLCL NFTYYYLGGI HLKISSNDNR TYKSLTLNNG LKVLLANDMS SDKAAASLTV
NTGHFDDPKD RQGMAHFLEH MLFLGTENMP KPGYFSQFIN QAGGQSNAWT GTEHSCYFFD
CHQHHFFKAL ELFSDFFIAP LLDASQTENE RNAIDAEFKM KIKDDGRRIY QVHKETTNPQ
HPFTKFSVGN QDTLANKDHC IAEEVRAFFT HNYLAQWMTL VIVGPQPLDE LKMWAENLFS
QIKGNAKPKP PLTAPLYRSQ DLGLLLQITP RKHMQKLIIS FAMPCIKGLY KHKSMSFLAH
LLGYEGEGSL YSILKAQGWI NALSAGGGVS GSNFKDFNIS FALTDEGINY YEDVVEMAFE
YIALIKSQLH NLAILYKDKK TLLDIAFNNQ EPCRLLDWAS SVSVNMHHYE PQDYLYGDYI
MSEFNPTIFE QLCNFLSPHN MRLVLIHPQV TPEHTARWYN TPYKVEKLAR DWLNALAQID
SALPEMLLPT VNPYLQVENT LFDIEPATHK PELLKDKPGF SFWFKQDATF RVTKGHFYIE
IDSPVAVKST KSMALTRLFA DLLMDGMAEQ FYPAELAGLN YHISSHQGGL TLHTAGLSGN
QLVLAMELLT AILKQPISAT RFAEYKKQLI RHWKNHNQNK PVSELFGLLG AHLMPWNPDP
TALASALKTT CFNEFRHFKE AFFNSIYIKA FLHGNWQKQH ALSMQKEIRT LFSQSEILED
LKRPLNVLSA AEQINITQPD ADHAIVEYIQ ALNDSVTEKV SLMMLNQMIS QDYFDKLRTE
LQLGYLVGCG YAPFNTRAGV AFYIQSPNNK PDVLDKHHHE FIQSFTISIK ELTDTQWLEA
KKALRLQIAE KDKNLRLRAQ RFWIAITNDD FKFSMQKRLI SELDNLEKQD FMAFTQRIFA
HNYPRVKLRC N
//
