ID A2SHN6_METPP Unreviewed; 921 AA.
AC A2SHN6;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Putative zinc protease {ECO:0000313|EMBL:ABM95075.1};
GN OrderedLocusNames=Mpe_A2119 {ECO:0000313|EMBL:ABM95075.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM95075.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM95075.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CP000555; ABM95075.1; -; Genomic_DNA.
DR AlphaFoldDB; A2SHN6; -.
DR STRING; 420662.Mpe_A2119; -.
DR KEGG; mpt:Mpe_A2119; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_007487_1_1_4; -.
DR Proteomes; UP000000366; 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: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:SF21; PROCESSING PROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
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:ABM95075.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000366};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..921
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002645470"
FT DOMAIN 64..209
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 217..392
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 673..852
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 921 AA; 100701 MW; EFEC16929341EA0D CRC64;
MFSKYLVAGA LALVVMQVSP VVAAASKPIP PSGSVASPGL PRGVTAVTQV EGITEYRLTN
GLQVLLVPDA SKPTTTVNLT YHVGSRHENY GETGMAHLLE HLMFKGTPTT PNVWGEFTKR
GLRANGSTWF DRTNYFASFA ANDDNLRWFL SWHADAMVHS FIARKDLDSE MTVVRNEMEM
GENNPGRILY QKTLAAMYDW HNYGKDTIGA RSDVENVDIA RLQAFYRQYY QPDNATLVVS
GQFDTARVLA WVQQYFGKIP RPRRVLPTLY TLDAAQDGER ALTLRRVGGA PLLYAGYHVP
AAPDPEFAAI ELLALVLGDA PSGRLHKRLV EKQLAASVGA EPFGLHDPGA ALFVAQLAPE
QDVERARSEL IAVLESVAAE PVTAEELERA RAKWLKGWDL AFTNPETVGV SLSESVAQGD
WRLFFLIRDR VKATTLEDVQ RVAVERLLPS NRTLATYVPT DKPQRAPAPK AVDVAAQFKD
FKPQAGATAV AAFDTTPANI DAQTQRFALA SGMKVALLPK PTRGGAVNAV LSLHFGDEKS
LADQGEVPAL TAAMLDEGTA KLSRQQIRDR LDALQAEVAF SSGTGSVSAT IATKRENLPA
VIALVGELLR EPSFPPAVLE EQRSQALTGV EQQRKEPEAV VANAIDRHVN RYPRSDVRHA
KSFDELVADI RAATPDQLRA FHRRFYGASH AEFGASGDLD VPAVRQALEA AFGDWKSSEP
YARVSDPLAP VAPARLVLPT PDKQNAHMAV FLPVPLMDSD PDYAPLTLAN HLLGGGGSSR
LWVRIREKEG LSYGVYSYLA WNQDERNSPW QAQAIFAPQN RAKVEAAFRE EVARSLQDGF
TATELQEAQR GLISARRLSR AQDARLAAGL ASNLRLDRTF AISQQVDDAI AAATLEQVNA
ALRKYIRPEA FVYGFGGDFK E
//