ID A0A0Q5HU76_9BURK Unreviewed; 939 AA.
AC A0A0Q5HU76;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KQQ97604.1};
GN ORFNames=ASF77_01710 {ECO:0000313|EMBL:KQQ97604.1};
OS Massilia sp. Leaf139.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ97604.1, ECO:0000313|Proteomes:UP000051760};
RN [1] {ECO:0000313|EMBL:KQQ97604.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ97604.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ97604.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ97604.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQQ97604.1}.
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DR EMBL; LMOJ01000001; KQQ97604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5HU76; -.
DR STRING; 1736272.ASF77_01710; -.
DR Proteomes; UP000051760; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF21; PROCESSING PROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
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:UP000051760};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 50..136
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 203..381
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 521..658
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 675..850
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 479..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 102557 MW; 25F4D62E0570A3FB CRC64;
MASTFAGTAA APAHAAAVQK AAAKAAAPAL KVDFQKFTLP NGLEVIFHID RSDPVVAVNL
TAHVGSSREK VGRTGFAHLF EHLLFLESEN LGKGGLDKMT ARIGGSGANG STSQDRTNYL
QTVPKDALEK MIWAEADKLG WFINTVTDPV LAKEKQVVKN EKRQGVDNAP YGHTRYVINK
ALYPADHPYN WQVIGSLDDL QNATLDDVKE FFRLWYVPNN VTLVLAGDFD PVQARKWVEK
YFSEIKRGEA VKPMVKRPGV VKQTVKLAHE DNFAKLPELT MAWPTVEDLH PDSYALEVLA
EYLSQTKRAP FYQVLVEDAK LAPNVQIGNQ ASELAGQFML RIRAFENKPL DQVAGAVDQA
FAKFEKEGIA EKDLNRIKAG LETRFYNSVS SVLGKSALLA EYNYLTGNPG YVSEGVRKTL
AVTGADVRRV YDTYIKGKPF VATSFVPKGK LALALTGSSK AEVVEEKVVQ GAENAVDPSA
NAEYAKTPSS FDRSKEPPYG ETPAVKVPAV WNTTLANGMR VAGIENREVP LVQFDIAIDG
GLLLDKLDKV GVANLMARLM TQGTATKTPQ ELEEAILQLG ATINVTARTE DVRISVTTLA
RNYAATLDLV QEILLQPRWD EKEFALIKQS VLSQIRQQEA DPNALASINF AKLVYAKDDL
RSRNILGTAE TVNAITIDDL KAYYAANLTP SNARMHVVGA LPKATVTRSL AKLERAWKAK
PVALPAPSKV ASGAPAKVYF VDVPDAKQSV LHVGYRALAV TDPDYYPATV MNYILGGGGF
ASRLTQQLRE GKGYTYGINS SFSGTGSAGP FIIASGVRSN VTLESAQLVK EILQTYPSTY
SAADLETTRN FLVKSNARAF ETAAAKLGML DNISKYGWRP DYVKEREQIV KAMTLPRIHA
LSEKYLDPSK MVWLVVGDAK TQLPRMKALG LDEPVLISK
//