ID A0A066UEJ9_9GAMM Unreviewed; 465 AA.
AC A0A066UEJ9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=M16-like peptidase {ECO:0000313|EMBL:KDN25836.1};
GN ORFNames=MBO_01530 {ECO:0000313|EMBL:KDN25836.1};
OS Moraxella bovoculi 237.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=743974 {ECO:0000313|EMBL:KDN25836.1, ECO:0000313|Proteomes:UP000035860};
RN [1] {ECO:0000313|EMBL:KDN25836.1, ECO:0000313|Proteomes:UP000035860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=237 {ECO:0000313|EMBL:KDN25836.1,
RC ECO:0000313|Proteomes:UP000035860};
RX PubMed=24970830;
RA Calcutt M.J., Foecking M.F., Martin N.T., Mhlanga-Mutangadura T.,
RA Reilly T.J.;
RT "Draft Genome Sequence of Moraxella bovoculi Strain 237T (ATCC BAA-1259T)
RT Isolated from a Calf with Infectious Bovine Keratoconjunctivitis.";
RL Genome Announc. 2:e00612-14(2014).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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:KDN25836.1}.
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DR EMBL; AOMT01000005; KDN25836.1; -; Genomic_DNA.
DR RefSeq; WP_036362357.1; NZ_AOMT01000005.1.
DR AlphaFoldDB; A0A066UEJ9; -.
DR eggNOG; COG0612; Bacteria.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000035860; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
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:UP000035860};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..465
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001627186"
FT DOMAIN 53..170
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 207..386
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 465 AA; 52440 MW; BCDFFED060C78C05 CRC64;
MFLRTKLSMA MIVGVLSLTA CQSLPSDTAL ASQTTPVKQT NYHEATLDNG LHIVIKKDAR
APIAMTQLWY KVGSNDEPIG KGGMSHFLEH MMFKDNAHLK RTEFNRLISE FGGQNNAFTS
DTHTAYYELF PASYYPLAMQ MESFRMQDLH LKDSEVAIEK EVIKEERRQR TEDNPLSKAY
EEFIALSQPD SPKFRPVIGS MADIENLSTA DLQAWYDTYY APNNATLVVV GDVDYDEVIN
NAKKYFGDKK AINIPERVMP TQPTHQGYRH ATTEQAVKLP SLMMAYNVPS ITTSDKQTAH
ALSLFQYALD GDMSSYFERV LVREKQLFSQ IYASYDAFDR GDGLFFIQAV PRQGVDLHTA
EQAILDVINA AKNTPITDQQ MTRITTSLLS ELTFAQDSIT AQAQIIGRLA NMGLPVDSYD
RLPEDLKQIH PAKVQEVAKH YLTKDNLTTL YILPKDNDSD NQSTQ
//
