ID A0A396U5T5_9GAMM Unreviewed; 962 AA.
AC A0A396U5T5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=D1094_11985 {ECO:0000313|EMBL:RHW75831.1};
OS Colwellia sp. RSH04.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=2305464 {ECO:0000313|EMBL:RHW75831.1, ECO:0000313|Proteomes:UP000266369};
RN [1] {ECO:0000313|Proteomes:UP000266369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSH04 {ECO:0000313|Proteomes:UP000266369};
RA Meng X.;
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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:RHW75831.1}.
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DR EMBL; QXIO01000006; RHW75831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A396U5T5; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000266369; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000266369};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 63..178
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 225..404
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 408..683
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 687..863
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 962 AA; 108620 MW; F7338FF7837F24B2 CRC64;
MKYWNISLLV VLLSACQQSN HINQPNTSAN TVATNPVEQT GIVKSKKDSR LYQAMMLDNG
LEVMLVSDPS IEKSAAALSV AAGSLQEPEA FGGLAHYLEH MLFLGTKTYP DVNEYNEFIS
RNGGSENAYT ELDHTNYMVS VNNDAYGEAL KRFSRFFYEA LLDEQYADKE RNAVHSEWSQ
KGPNDWVIMG QLDGYTLNPD HPISQFNWGN LESLADKDNQ KLQDLLVDFY NKYYSANLMK
AVMISHLPLA QMQKLAKDNF GKITNKNTPK PVITKPVAQS EQLKKIVHYV PQTDMKQLQV
KFVINDNSEQ FAVKPNFYLR YLLSNEMPGT LASTLRELGY TENLWASSNP SEYGNAGSFT
IYATLTETGL KNRNSIVGAI FDYLALIKAQ GIDAKYFKEI KQSLSNSFQF KEKIDDYSYA
MQIAANLQDT PASYVLSSDY EYQRFNSAAI NAVLEQLTLD NARIFYIDKA QPTNTEMDFF
VGKYQVESIT KEISQQWQKA SEEINLSLPS PNTLMPENFD IETAQYIDKP KTLINEQGLN
VYLAHSKHFT QPKGSFSANF NSGFDKESPR NHVLAALLSD GLRMDLTALS SEASAAGMRL
NVGSYNGLYL TASGFTNKQQ QLLANAYQSI LNYQVSSAQL DNLKASYISG IESKQKYMLL
NQLFPQFNKI VNLDEFSDTS LLAEVASITP NELLTFRDQL LNKAKLNIFA FGNYNEEQVI
KTAKYLESLL PKSRQVSDIY FTKTFKPTKG TVINWQQDVD MNDIAVGDFY MAPFEVKQYA
AAQVLQKVLK PALFNQIRTE EQLAYSVGFF SQALREQILL GFYIQSPAKG PAAVIDRIAA
FRHNFTTELA ELSAEEFDTI RKSVLISLTQ PPKNLAEESS AFVSDWRKNK LSFDSKAKLI
SAIKSLELAD IKHLYQQLNQ DNAFGRVMVQ MRGKNFKDQP FVEPDNVKQI TDVNDFHHSI
SQ
//
