ID I3C0I2_9FLAO Unreviewed; 948 AA.
AC I3C0I2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Putative Zn-dependent peptidase {ECO:0000313|EMBL:EIJ37125.1};
GN ORFNames=JoomaDRAFT_0063 {ECO:0000313|EMBL:EIJ37125.1};
OS Galbibacter orientalis DSM 19592.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Galbibacter.
OX NCBI_TaxID=926559 {ECO:0000313|EMBL:EIJ37125.1, ECO:0000313|Proteomes:UP000004690};
RN [1] {ECO:0000313|EMBL:EIJ37125.1, ECO:0000313|Proteomes:UP000004690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19592 {ECO:0000313|EMBL:EIJ37125.1,
RC ECO:0000313|Proteomes:UP000004690};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Chertkov O., Ovchinnikova G., Kyrpides N., Mavromatis K.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Improved High-Quality Draft genome of Joostella marina DSM 19592.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; JH651380; EIJ37125.1; -; Genomic_DNA.
DR AlphaFoldDB; I3C0I2; -.
DR STRING; 926559.JoomaDRAFT_0063; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_008156_0_0_10; -.
DR Proteomes; UP000004690; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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; IPR007863; Peptidase_M16_C.
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 SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
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:UP000004690};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..948
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003668661"
FT DOMAIN 59..171
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 210..394
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 703..878
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 948 AA; 110331 MW; 542351B18C0D5271 CRC64;
MNYLYYLLVY ILLAGANNLN AQEPENLNKE DSTLTSAVYS NQLNNGLNYY LKPIKGTTNI
SLNLWLRAGF NEEASDQQDI SHAVEHLAFR SSVHFPEGIK NTQKLAALGI EKNDATAGTA
YHYTRYTISI PSESQRALHN GLLWFKDILN GLLLTTEDIN IERTTLRQEF LHRAGNDLSN
RIVKSQIDAK RNSCKKSQEF FLEDNANFPP QVVRQFYKKW YRPDLAAVSV IGDIPNLEII
KKEIHQLFSD LPKPSTPIRK LNCDVLYYEQ EPKFYKVERP SSKPEEELSQ EVEIHLDYRD
SLMYKEIQNV KGLKRRILFE TISAILNKRF KEQQSIYCPK FNFWMKYKEN PFFLTSQISV
TPGYEKLALE RFFELVHQLK KYGITEKEWA TVKNDRKTQK ANHNRHWVEE IIKFDVYGEA
LPNDKIEKLN EWWQHLSRSE FNSYLQELIR EMPEDIGIIA HKNQKAFKLK EKEVRSWIKQ
SWISEIDPYN PPKIPEHLMD GSHLDKNISN KKLMYSSTKM GTKELTLENG VKIIFLQDSS
IAPIKNPTIT LHGFVPYGAA NFPKEDYHSV INAPFIIENS GVGSFDKFQV NRYLSQSEDP
INLHSYINYS ESGFTGYAKL HSFNDLLQMI YLYTTQPRKN KLAFKDWKER KRKEYSNPPY
GLGNVDMINE IKAILKDSSF INMGTFQHQG LSNIDLNKTY TSYQNIFGNA EAFTFILYGN
YSIEMLLPDI QKYLGNLPTN KEGILEKSTN DVPSLLNGGP LYKKLNLGYL MQSDNYQMYF
LSRKPEVFTW KKKLQLGILG KILDQMLFLD LRYKKGYGIY SPHATTEYNI SLSRFMTSLR
IECEPFESTA IQDDIHKIIK DIQTGKISSD HFENAKANVS SNNSSSLYRQ EQRLFEYYRY
QIPWISKTDI DRVISETTLK DIVALAKEVF KPKNQYEFLV PSKNSVVK
//