ID A0A381GZ59_CITKO Unreviewed; 962 AA.
AC A0A381GZ59;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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 Name=ptrA {ECO:0000313|EMBL:SUX84006.1};
GN ORFNames=NCTC10810_01238 {ECO:0000313|EMBL:SUX84006.1};
OS Citrobacter koseri (Citrobacter diversus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=545 {ECO:0000313|EMBL:SUX84006.1, ECO:0000313|Proteomes:UP000254077};
RN [1] {ECO:0000313|EMBL:SUX84006.1, ECO:0000313|Proteomes:UP000254077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10810 {ECO:0000313|EMBL:SUX84006.1,
RC ECO:0000313|Proteomes:UP000254077};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-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}.
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DR EMBL; UFWJ01000004; SUX84006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A381GZ59; -.
DR Proteomes; UP000254077; 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, ECO:0000313|EMBL:SUX84006.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SUX84006.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000254077};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..962
FT /note="Protease 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030069902"
FT DOMAIN 54..191
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 216..393
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 400..675
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 681..857
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 962 AA; 107822 MW; 0555655E78AC0511 CRC64;
MPRSTWFKAL LLFVALWAPL SQADTGWQPL AETIRKSEKD TRQYQAIRLD NDMVVLLVSD
PQAVKSLSAL VVPVGSLEDP DEHQGLAHYL EHMSLMGSKK YPQPDSLAEY LKMHGGSHNA
STAPYRTAFY LEVENDALSG AVDRLADAIA APLLDKKYAE RERNAVNAEL TMARTRDGMR
MAQVSAETIN PAHPGSRFSG GNLETLSDKP GNPVQQALQA FHEKYYSANL MKAVIYSNKP
LPELARIAAE TYGRVPNKNI KKPEITVPVV TDAQKGIIIH YVPALPRKVL RVEFRIDNNS
AQFRSKTDEL VTYLIGNRSP GTLSDWLQKQ GLVEGIRADS DPVVNGNSGV LAISATLTDK
GLANRDDVVA AIFSYLNLLR EKGVDKRYFD ELAHVLDLDF RYPSITRDMD YVEWLADTMI
RVPVEHTLDA VNIADQYDAA AVKSRLAMMT PQNARIWYIS PKEPHNKTAY FVDAPYQVNK
IDDKTLADWQ QKAQGIALSL PELNPYIPDD FTLIKPEKEY PHPELIVDEP DLRVVYAPSR
YFASEPKADV SVILRNPKAM DSARNQVMFA LNDYLAGIAL DQLSNQASVG GIGFSTNANN
GLMLNANGYT QRLPQLFQAL LEGYFSYTAT EEQLEQAKSW YAQMMDSAEK GKAYDQAIMP
VQMLSQVPYF QRDERRKLLP SITLKEVMAY RDTLKAGARP EFLVIGNMRE AQVKTMARDI
QQQLGANGSE WCRNKDVLVD KKQSVIFEKA GSSTDSALAA VFVPTGYDEY ASSAYSAMLG
QIVQPWFYNQ LRTEEQLGYA VFAFPMSVGR QWGMGFLLQS SDKQPSYLWE RYKAFFPTAE
AKLRAMTPEE FAQIQQAIIA QMLQAPQTLG EEASKLSKDF DRGNMRFDSR DKIVAQIKLL
TPQKLADFFH QAVVEPQGMA ILSQVSGSQN GKAEYVRPEG WKVWENVSAL QQTLPLMSEK
NE
//
