ID G4A751_AGGAC Unreviewed; 930 AA.
AC G4A751;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Probable zinc protease {ECO:0000313|EMBL:EGY34255.1};
GN ORFNames=SC1083_0642 {ECO:0000313|EMBL:EGY34255.1};
OS Aggregatibacter actinomycetemcomitans serotype e str. SC1083.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=907488 {ECO:0000313|EMBL:EGY34255.1, ECO:0000313|Proteomes:UP000005508};
RN [1] {ECO:0000313|EMBL:EGY34255.1, ECO:0000313|Proteomes:UP000005508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC1083 {ECO:0000313|EMBL:EGY34255.1,
RC ECO:0000313|Proteomes:UP000005508};
RA Chen C., Kittichotirat W., Asikainen S., Bumgarner R.;
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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:EGY34255.1}.
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DR EMBL; AEJM01000016; EGY34255.1; -; Genomic_DNA.
DR AlphaFoldDB; G4A751; -.
DR SMR; G4A751; -.
DR PATRIC; fig|907488.3.peg.632; -.
DR Proteomes; UP000005508; 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:SF34; ZINC PROTEASE PQQL-LIKE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
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, ECO:0000313|EMBL:EGY34255.1};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..930
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003461182"
FT DOMAIN 55..174
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 213..394
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 688..861
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 930 AA; 107201 MW; ABC5EFC5332FC1D2 CRC64;
MRNQKTMKKL TALFVLLCSF RLLMACQTGM DPNALPFDPD IKHGKLTNGL QYYTLNNRDP
KDRVYIRLVV NAGSMHEDDD QKGIAHLVEH MAFNGSKKYP ENTIINALEK LGMKFARDIN
AFTDFENTVY TLNLDGNSPQ KLSLAFDVIN EWMNHLTILP KDLDGERGVV QEEWRRRLSP
MLRLGDKKSA IEMAGSRYVL RDPIGDMNII RHISRDRVAD FYHKWYRPDN MSLIVVGDID
AHKIAQLISQ QLDKPSSRTQ RPLDKIDFSI PLIHHWRVAS IAEQSTNIPA LELSFFEEDK
QKETVIGYKQ DLIQQIVTRL VNLRLQKWEE SQNNWLDSAN FYRSHLGKQT LQSVFSLQLI
DTNYLKNITA LFAFIAEIKQ HGFTADELNG EIARLHNLNE KQQNIRPGSL KIANDLIAIA
ANHQIMLSTK ERYNLNRRFL NEIKVTDLNA TFNQMLALNA KLLLITQPLP EKKLPFDADY
IEQRWNQAMH SSQNQWENKK HIIKQPHFEF KDGSLVLEKH WDKGDIDEFR LSNGAKLIYH
YSNKTPNQVH FRAVTSGGLR SVPNQDYHLL RTAITLVDDT GTGELTQADV NNLFGQSPLV
LATVIDDDKQ GFTGVAKPQD LSSLLTLFRL KLQSAPVSDN VLQKYHRETQ DYFKQIDAET
KFMQAISYLR RPNTATVYTQ NQNEQLSFTA AQLSQIYQEK ILGKTDFTYF IIGDISRSEV
EKLAKRYLAT VEIKTQARAY QPGYIHTPKK AFIMRGLSEP RADVEIYLTA ENQWHPEQKY
ALEILAEIVQ EKLRLVLREK VSGIYSVNSW FSQDPHTPQI EGKIAFSCAP NRAEELIKLT
HQILDEIIEN GIDETLLRKK QAEQQQLIKR QFDSLVSVAG MIEDSYWQQG NPQSVYLYQR
LEQLADKPHL EALARKVLVK AARFEAILRQ
//