ID A0A0N0KCG7_9SPHN Unreviewed; 935 AA.
AC A0A0N0KCG7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KPF89285.1};
GN ORFNames=IP83_03035 {ECO:0000313|EMBL:KPF89285.1};
OS Novosphingobium sp. AAP93.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523427 {ECO:0000313|EMBL:KPF89285.1, ECO:0000313|Proteomes:UP000037906};
RN [1] {ECO:0000313|EMBL:KPF89285.1, ECO:0000313|Proteomes:UP000037906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP93 {ECO:0000313|EMBL:KPF89285.1,
RC ECO:0000313|Proteomes:UP000037906};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:KPF89285.1}.
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DR EMBL; LJHZ01000016; KPF89285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0KCG7; -.
DR STRING; 1523427.IP83_03035; -.
DR PATRIC; fig|1523427.4.peg.1203; -.
DR Proteomes; UP000037906; 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:SF17; PROTEIN YHJJ; 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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 45..168
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 205..275
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 698..859
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 935 AA; 100997 MW; 87392FB7976163B0 CRC64;
MLVLVAVPLA PAAAKPAPVW AFEKSDLAPD PGFRFGRLPN GMRYVIRHNA TPKATAEVRL
QIDAGSLDER DSERGFAHFV EHMAFNGSTH VPEGEMVKLL ERAGLAFGAD TNAQTSFEYT
LYMLSLPRAE PALLDTALML MRETASELSF APEAVARERG VVLSELRDGQ GYALENNKDQ
MAFLYPAANF RDRLPIGTVE SLKAATAEAL RAFWAREYVP AKATLIVVGD FDADAVEAAI
KARFADWPAR KPAKRPDQGR VFPDQQGASR IHLDPALSER VTVSRHGRWR KEPDTEESRR
VNLLRQIGYG VINRRMQRLS RIAQPPFRGA GVGTSEVFHI GRTTNLVVDT ADKGWRKGLL
AAARVYREAL AKGFTEAEVA EQLAGTRTAI ENAAASADTR SNDALVGAVL QLLRDDKVPT
TPASSLERLN RHAASFTPAA VLAALRADAI PLANPLIRFQ GRSAPEGGGQ ALRAAWNEAQ
AAPLQAATST TSGTFAYTDF GPPGAVASDT TRADFGLRQI RFANGVRFNL KRTDLEADRV
LLRLHIDGGE LLDTKANPTA TEMTAMLPTG GLGKHSLDDL QTLLAGRSVG TNIASSGDTF
AMAAATTRRD LELQLDLMAA QITDPGWRTS AGVIYHQTMT NFFARIDATP SSALANRLPS
LLSGGDPRFT VQAPETYQAL TMARLKADIG GRLAHGAIEL TMVGDFDPEA AVAMVARTFG
ALPPREPDFL PYTAERERSF TPKRGITVIR HKGAPNQAIV RYVWPTTDDS DPVTSIGLEL
LQEVTGIEVL DTVREALGKA YSPGAASSLS RVWRGWGTFT VNASVDLADV AATRSAIEST
IAGLAAKPVD DDILARARAP MRERIDNLLK TNGGWLALVD RAQSQPDRIA RYQLARQRLD
ALTAADLQAL ARRYLAPDQA VVALVLPEGA PAPAR
//