ID A9E0E7_9FLAO Unreviewed; 990 AA.
AC A9E0E7;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Peptidase, M16 family protein {ECO:0000313|EMBL:EDP95833.1};
GN ORFNames=KAOT1_05497 {ECO:0000313|EMBL:EDP95833.1};
OS Kordia algicida OT-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Kordia.
OX NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP95833.1, ECO:0000313|Proteomes:UP000002945};
RN [1] {ECO:0000313|EMBL:EDP95833.1, ECO:0000313|Proteomes:UP000002945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT-1 {ECO:0000313|EMBL:EDP95833.1,
RC ECO:0000313|Proteomes:UP000002945};
RX PubMed=21622754; DOI=10.1128/JB.05241-11;
RA Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.;
RT "Genome sequence of the algicidal bacterium Kordia algicida OT-1.";
RL J. Bacteriol. 193:4031-4032(2011).
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:EDP95833.1}.
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DR EMBL; ABIB01000006; EDP95833.1; -; Genomic_DNA.
DR RefSeq; WP_007093668.1; NZ_DS544873.1.
DR AlphaFoldDB; A9E0E7; -.
DR STRING; 391587.KAOT1_05497; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_306466_0_0_10; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000002945; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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 PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 2.
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:UP000002945};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 64..109
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 271..439
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 567..696
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 772..889
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 990 AA; 113037 MW; 61535FA4ECEBF725 CRC64;
MKKINLLLLI VFTLTIFSCK ENNDVASNEV KVSQQKDANG FSYETVANDP TGLRLYTLDN
GLKVYLSKNS DEPKIQTYIA VRAGSVYDPK ESTGLAHYLE HMVFKGTDEI GTLDWEKEKE
YLQQISDLYE EHRAEKDPEK KKEIYKKIDE VSLEASNYSI ANEYDKMTSS LGATGTNAHT
WHEETVYKNK IPANELDKWL DLESERFGQL VLRLFHTELE AVFEEFNRGQ DNDGRKSYAA
MLDGLFPNHP YGQQSTIGIG EHLKNPSMVA IHNYFNKYYV PNNMAVVLVG DIDFDETIQK
VANTFGKMEK KEVTHPTLPK EQPIASPVVK EVFGPTAENI SISFRSGGVN TKDEKYVTLV
DMILSNGNAG LIDLNLNQKQ AVQYARSSPT FLNDYGYHTL SGYPKTGQTL DEVKNLLLAQ
IEKLKKGEFE DWMIDAVIND LKLSQTQQYE NSTALASAYY NAFIHHEDWS KKVKFLDDLK
KITKEELVEF ANKFYKDNYV VTYKRKGADN SIVKVENPGI TPVNLNRDKS SAYMKAFNAR
EATPLQPKYV DFKSAIKETE LDNGIKVSYI ENEQNDLFDM NIIFDMGSDN DKKLGLGVGY
MEYLGTDKYS AEELKKEFYK LGISYYVSTG AEKSYVGLNG LKENLPEGLK LLSHLWNNAV
PNQEAYDKYV TQILKSRQNT KTRKGSILQR GLMSYAKYGE NSRLRNIFSN SELNEMNPQE
LVDLVKDFKN YNQRIFYYGK DVDAAVAALN EHHKVADDLK EYPAATEYTE LETGGNVFFV
DYDMVQAEMM FLAKGEPFKA ENMAASTLFN TYFGSGLSSI VFQEIRESKS LAYSAYSYYA
EANDKNDSNY VMAYIGTQAN KMPQAVDAML SLMNDMPEAE EQFNAAKEAT LKKLAAQRIT
KSNIFWTYER LQKLGIDKDH REEMYKAIEK MTLADLKEFF NENIKGEQYN VMVIGNKKDV
DMKALSKLGK IQEMDIDYLF NYEKPKDIKQ
//