ID Q60CP2_METCA Unreviewed; 459 AA.
AC Q60CP2;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Peptidase, M16 family {ECO:0000313|EMBL:AAU90786.1};
GN OrderedLocusNames=MCA0063 {ECO:0000313|EMBL:AAU90786.1};
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233 {ECO:0000313|EMBL:AAU90786.1, ECO:0000313|Proteomes:UP000006821};
RN [1] {ECO:0000313|EMBL:AAU90786.1, ECO:0000313|Proteomes:UP000006821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath
RC {ECO:0000313|Proteomes:UP000006821};
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(2004).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017282; AAU90786.1; -; Genomic_DNA.
DR RefSeq; WP_010959435.1; NC_002977.6.
DR AlphaFoldDB; Q60CP2; -.
DR STRING; 243233.MCA0063; -.
DR MEROPS; M16.019; -.
DR KEGG; mca:MCA0063; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_1_0_6; -.
DR Proteomes; UP000006821; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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: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; 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; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006821};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..459
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004266542"
FT DOMAIN 34..180
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 189..370
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 459 AA; 50767 MW; 8BC6EFE9C88BB599 CRC64;
MSIPRLGFLL MALPLAAPAA PPQVHEFTLA NGLRVLVQED HRAPVAVSQV WYKVGSSYEY
GGITGVSHML EHMMFKGTKK HPPGEFSRII AANGGSENAF TGQDYTAYFQ TLERSRLPVS
LELEADRMRN LRLLQDEFVK EQQVVIEERR LRTEDQPHAR MEEHFHAVAF TDSPYRNPVI
GWPEDVAGLT LDDLSAWYQR WYAPNNATLV VVGDVAPGEV FELARKHFGP LKPAKLPALK
PQGEVPQLGL RRMVVKVPAK LPHLEMGYKV PSLKTAAAEW EAYALEVAAG ILDGGNSARL
TSRLVRGRQI AAGVGAGYDL YARLSPLFSL EGTPAQGKTV AELEAALLEE VRRLREEPVA
EDELARVKAQ VLASNVYQRD SVFYQAMQLG MAETVGLGWR KVEEYVDKIN AVTAEQVREV
ARKYLIDDGL TIAHLEPQPI PEGAKIQEGP EGMGGGHVR
//