ID   A8T554_9VIBR            Unreviewed;       925 AA.
AC   A8T554;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   24-JAN-2024, entry version 53.
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=AND4_15615 {ECO:0000313|EMBL:EDP59201.1};
OS   Vibrio sp. AND4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=314289 {ECO:0000313|EMBL:EDP59201.1, ECO:0000313|Proteomes:UP000005159};
RN   [1] {ECO:0000313|EMBL:EDP59201.1, ECO:0000313|Proteomes:UP000005159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AND4 {ECO:0000313|EMBL:EDP59201.1,
RC   ECO:0000313|Proteomes:UP000005159};
RX   PubMed=20436956; DOI=10.1371/journal.pbio.1000358;
RA   Gomez-Consarnau L., Akram N., Lindell K., Pedersen A., Neutze R.,
RA   Milton D.L., Gonzalez J.M., Pinhassi J.;
RT   "Proteorhodopsin phototrophy promotes survival of marine bacteria during
RT   starvation.";
RL   PLoS Biol. 8:E1000358-E1000358(2010).
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:EDP59201.1}.
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DR   EMBL; ABGR01000005; EDP59201.1; -; Genomic_DNA.
DR   RefSeq; WP_009842566.1; NZ_ABGR01000005.1.
DR   AlphaFoldDB; A8T554; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000005159; 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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          21..159
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          182..360
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          366..638
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          648..812
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   925 AA;  105674 MW;  879B1302984CA0D2 CRC64;
     MHLSPNDSNQ YRYITLSNGL RVLLIHSDTA QQSAAALAVN VGHFDDPIDR QGLAHYLEHM
     LFLGTEKYPK VGEFQSYISQ HGGANNAWTG TEHTCFFFDV TPNAFEGALD RFSQFFAAPL
     FNEEALDKER QAVDSEYRLK LNDDSRRLYQ VNKEVINPKH PFSKFSVGNL ETLCDRGEKS
     IRDEIVEFHQ SQYSADLMTL TSFGPQSLDE QQAWVEIMFS GIPNHQLRGK SIDVPINTEE
     STGILVQVEP IKELRKLILT FPMPGMDAHY SVKPLSYFAH LLGYEGRGSL MLQLKEKGWI
     TSLSAGGGAS GSNYRDFTVS CTLTPRGLDC IDDIVQAVFQ YLTMIKQDGM DEWRYKEKQA
     VLESAFRFQE PSRPMDLVSH LVINMQHYQP EDTVYGDYKM TGYDEKLQRS LLQYLSVENV
     RITLIAKGLE YRQNAEWYFT PYSVTPFSAE QCRFYQQIDP SWQFVLPEKN PYICYDLDPK
     PFENGGSLPE LVEDLEGFRL WHLQDGEFRV PKGVVYVAID STHAVASPKN IVKTRLCVEM
     FLDSLAEETY QAEIAGMGYN MYAHQGGVTL TLSGFSQKLP QLLQVILHRF AAREFSPERF
     ETIKQQLLRN WRNSSQDRPI SQLFNALTGL LQPNNPPFAV LSEALEEIEV DELSVFVESI
     LAELHVEMFV YGDWQRQQAH DMASTLKDAL RVKEQHYEEA LRPLVMLGKN GSFQREVNCN
     QQDSAVVIYH QCEDISPHNI ALYSLANHLM SATFFHEIRT KQQLGYMVGT GNMPLNRHPG
     IVLYVQSPSA APAELVTSID EFLNAFYMVL LELNEYQWHS SKRGLWNQIA TPDTTLRGRA
     QRLWVAVGNK DTDFNQREKV LDELKELTRT DMIRFVVNEL KPRTANRLVM HSQGTAHQDA
     PRITLGQEIG SIDEFQLRPK DFGLG
//