ID G0IWE3_CYCMS Unreviewed; 676 AA.
AC G0IWE3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Peptidase M3A and M3B thimet/oligopeptidase F {ECO:0000313|EMBL:AEL27131.1};
GN OrderedLocusNames=Cycma_3408 {ECO:0000313|EMBL:AEL27131.1};
OS Cyclobacterium marinum (strain ATCC 25205 / DSM 745 / LMG 13164 / NCIMB
OS 1802) (Flectobacillus marinus).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=880070 {ECO:0000313|EMBL:AEL27131.1, ECO:0000313|Proteomes:UP000001635};
RN [1] {ECO:0000313|Proteomes:UP000001635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25205 / DSM 745 / LMG 13164 / NCIMB 1802
RC {ECO:0000313|Proteomes:UP000001635};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Cyclobacterium marinum DSM 745.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR EMBL; CP002955; AEL27131.1; -; Genomic_DNA.
DR RefSeq; WP_014021421.1; NC_015914.1.
DR AlphaFoldDB; G0IWE3; -.
DR STRING; 880070.Cycma_3408; -.
DR KEGG; cmr:Cycma_3408; -.
DR eggNOG; COG0339; Bacteria.
DR HOGENOM; CLU_001805_4_0_10; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000001635; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06456; M3A_DCP; 1.
DR Gene3D; 1.10.1370.40; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR034005; M3A_DCP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000001635};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 225..673
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 676 AA; 76974 MW; 1108E76DC22CF128 CRC64;
MNPLLAKFNT PFETAPFDKI KNEHFLPAIQ NGIAEVKEEI KKIKTSTPPD FENTIVALEN
SGEKLSRAAS IFFNINAAET NDEIQQLARE ISPLLSAHSN DILLDETLFK RVKAVFDQRD
QLKLTPEQST LLEKSYKSFI RNGALLKGDD KDRLRAIDQE LSKLGLHFGE NVLKETNKYE
LVVAEAKDLE GLPDGLIEAA AQTAQEKGKE GKWIFTLAFP SYVPFMTYAK NRELRKELYI
AYNTKSAKGD ELDNRQIIKN ILKLKDERAK LLGYDNYADF VLEERMAEGG EKVLSFLDEL
LEKAKPRAIS ELKELEAFAK KTDGIEKLFK WDISYYAEKL KMEKYAVDDE LLKPYFELNR
TIDGVFTTAE KLYGITFKEN KAIPVYHPDV KAYEVKDEKG DHLAVFYADF FPRAGKRNGA
WMTAYRGQRK IGNKENRPHV SIVCNFTKPT KTKPSLLTFN EVTTLFHEFG HALHGMLAQG
TYGSLSGTNV YWDFVELPSQ IFENWCYEEE CLDLFAKHYE TGEPIPKSYI ENIKKAANFH
QGFQTARQIS LGQLDMAYHT TAPDAIDDVF EFENDVMKPT ALLDPVPNTM ISTSFSHIFQ
GGYAAGYYSY KWAEVLDADA FELFQEKGVF DKATAKSFKE NILSMGGKEH PSILYKRFRG
RAPKPDALIK RAGLQV
//