ID A0A0F4QK97_9GAMM Unreviewed; 895 AA.
AC A0A0F4QK97;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=TW77_14435 {ECO:0000313|EMBL:KJZ07700.1};
OS Pseudoalteromonas rubra.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=43658 {ECO:0000313|EMBL:KJZ07700.1, ECO:0000313|Proteomes:UP000033452};
RN [1] {ECO:0000313|EMBL:KJZ07700.1, ECO:0000313|Proteomes:UP000033452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2471 {ECO:0000313|EMBL:KJZ07700.1,
RC ECO:0000313|Proteomes:UP000033452};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJZ07700.1}.
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DR EMBL; JXYA01000032; KJZ07700.1; -; Genomic_DNA.
DR RefSeq; WP_046005693.1; NZ_JXYA01000032.1.
DR AlphaFoldDB; A0A0F4QK97; -.
DR PATRIC; fig|43658.5.peg.3054; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000033452; 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:UP000033452};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 22..156
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 181..347
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 366..650
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 654..815
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 895 AA; 102333 MW; 60F9DF395A230C8A CRC64;
MKLSNNDKRN YRHLTLDNGL KILLVEDTSS NKSAASLAIN VGHFDDPQSR QGMAHFVEHM
LFLGTQSFPV RGEFSQFVSQ AGGQSNAWTG TEHSCYFFDC RAPLFEQALE RFSEFFYAPL
FTEDALQDER NAIDSEFNLK VKDDNRRIIQ VHKETVNPAH PFAKFSVGNH NTLADHSGNF
KQEIEAFFDA HYQAQWMTLV LAGPHSLDEL ARLANRYFSA INGSNTPKPP IQVPLYRQQD
LGLLLHIEPR KHMQKLIVSF AMPDVERLYK FKSLSFLAHL LGYEGDGSLY AILKKNGWIN
ALSAGGGVDG SNFKDFNISF ALTDDGIEYY EDIVEMLFEY ISLITEQLAS LPALYEDKKR
LLELAFENQE QSKLLDWVSA LSINMHHYDD DDILYGDYCM TAFNHALHEE LMGLLSPHNM
RLILIHPDIT CENDATREVA QWYNTPYQVE QINAEWLQTL ANITTPLPEM RLPAANPYLA
FENRLYDIEP GRKTPTLLTD RPGFAFWFKQ DTRFRVTKGH FYLEIDSQRS VESHKSMAMT
RLFADLFMDS VAEQFYAAEL AGLSYHLSSH QGGLTLQTAG LSASQLKLVL QLVEALLKQP
ISATRFAEYK KQLIRHWKNH NKSKPVSELF SLLGAHLMPW NPTPEQLAKA LKNISFNEFC
LFREDFFKAI HIKAFMHGNW QLDHALDMQK QLHALFAYSE ILDDLKKPLN PITSHQQVHI
EKPGAEHAFV EYIQAPTASV EDKVKVMAFN QLVSQDYFES LRTQQQLGYL VGAGYAPFNT
RAGIAFYVQS SSYDSETLLQ RHHQYMADLI AQLDSYEATQ WAQVKAALHA QIAEKDKNLR
LRSQRLWIAI GTDDHTFAMQ EKLIAALDAL TFDTLKQDIV KLLSIERARI TLRCN
//
