ID A0A1T5END3_9GAMM Unreviewed; 964 AA.
AC A0A1T5END3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Predicted Zn-dependent peptidase {ECO:0000313|EMBL:SKB85491.1};
GN ORFNames=SAMN05660880_02927 {ECO:0000313|EMBL:SKB85491.1};
OS Luteibacter sp. 22Crub2.1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Luteibacter.
OX NCBI_TaxID=1283288 {ECO:0000313|EMBL:SKB85491.1, ECO:0000313|Proteomes:UP000191150};
RN [1] {ECO:0000313|EMBL:SKB85491.1, ECO:0000313|Proteomes:UP000191150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22Crub2.1 {ECO:0000313|EMBL:SKB85491.1,
RC ECO:0000313|Proteomes:UP000191150};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; FUYT01000013; SKB85491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5END3; -.
DR Proteomes; UP000191150; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..964
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012911011"
FT DOMAIN 45..182
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 202..375
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 518..639
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 673..853
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 964 AA; 103587 MW; C97EBF453F90DDD8 CRC64;
MKNRLTLLAA GLISFVGAAA AATTSPDAIP DIPYTRFQLP NGLTVVVHED HKAPVVAVSI
WYHVGSGDEP AGKTGFAHLF EHLMFSGSEN RKGTYFQPFE RAGATDMNGT TWFDRTNYFE
TVPTTAVDMA LWMESDRMGH LLGAIGQKEL DTQRGVVQNE KRQGENRPYG RVDENVLVNT
FPANHPYHHD TIGSMADLDA ASLADVKQWF HDYYGASNTT LVLAGDITVA QAKAKAEKYF
GDIPAGPPVP RQQAWITPVQ TSSRGTQHDQ VAQTRIVRTW IVPQLGTDDA VQLDLATTVL
GGGKTSRLYQ RLVYQDKIAD DVSLGISPFA LASQVQLTVD VKNGVDPAKV EAAVADVWKD
YLAKGPTDDE LLRAKVANRA GFVRGLEKVG GFGGKAVILA EGQVYRNDPE AYKKDLERAQ
KATTASVLAA SKTWLAKGDY TLTVLPAAPG FDPAAEDKAV VGLGDAQGRP AAVTPPAKTY
TVGKSEVDRS TGVPAVDTFP DLSFPKLQRG KLKNGIEVVL AERHTVPVTQ VQLLFNAGYA
ADQGRKLGTA SFTSALLEES TKSLDSVEVA RRKERLGAIV SSSCSLDNCS VGLNALNTDL
TPSLALFADI TRNPAFKADD IERVRGQWIA GIAQEKTEPT GLALRTLPPL LYGKDHAYGI
PFTGSGTEKA IASLTADDLA AFQRDYLRPD NVRIVVAGDT TLADILPKLD AVFGDWQAPS
TALPKKNIGE VAAQPRPRVF LINRTDAPQS LILAGLLAPS TKAKNALDLG IANGAFGGTF
TSRLNMNLRE EKRWAYGAGS MLSDAQGQRP LLFYAPVQTD KTAESAAEIL KEAKAVIGPK
PLTDEEIEKI RAQRVRALPG SFETTSAVLG AITGILIYDR PDDYVQTLKS RIEGVDRKDA
EDALSAVIHP DALTWVIVGD LRKIEAPVRA LNLGEVHVID ADGAPAKDTV PARAARSKPA
PSKK
//
