ID   A0A0N1JTN8_9NEIS        Unreviewed;       941 AA.
AC   A0A0N1JTN8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Protease 3 {ECO:0000313|EMBL:KPC55077.1};
DE            EC=3.4.24.55 {ECO:0000313|EMBL:KPC55077.1};
GN   Name=ptrA {ECO:0000313|EMBL:KPC55077.1};
GN   ORFNames=WG78_00420 {ECO:0000313|EMBL:KPC55077.1};
OS   Amantichitinum ursilacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chitinibacteraceae; Amantichitinum.
OX   NCBI_TaxID=857265 {ECO:0000313|EMBL:KPC55077.1, ECO:0000313|Proteomes:UP000037939};
RN   [1] {ECO:0000313|EMBL:KPC55077.1, ECO:0000313|Proteomes:UP000037939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IGB-41 {ECO:0000313|EMBL:KPC55077.1,
RC   ECO:0000313|Proteomes:UP000037939};
RA   Kirstahler P., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.;
RT   "Draft genome sequence of the Amantichitinum ursilacus IGB-41, a new
RT   chitin-degrading bacterium.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KPC55077.1}.
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DR   EMBL; LAQT01000001; KPC55077.1; -; Genomic_DNA.
DR   RefSeq; WP_053935811.1; NZ_LAQT01000001.1.
DR   AlphaFoldDB; A0A0N1JTN8; -.
DR   STRING; 857265.WG78_00420; -.
DR   PATRIC; fig|857265.3.peg.89; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000037939; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
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:SF34; ZINC PROTEASE PQQL-LIKE; 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, ECO:0000313|EMBL:KPC55077.1};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KPC55077.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037939};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..941
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005875153"
FT   DOMAIN          54..178
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          213..394
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          694..867
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   941 AA;  103074 MW;  16549B39A8D36CFC CRC64;
     MPLLHKLFAG SLLAASLSTF ALPALTDFPQ DHSDIKPDPA VTFGKLDNGI RYAILPNSEP
     KGRASLRLLV KAGSMNETDD QQGLAHFLEH MAFKGSTHYA PGTLVNYFQR LGMGMGSDAN
     ANTGFERTVY ELELPDTKPE TMTEGLQVFA DFSGGLLLKP DQIEGERGVI LSEKRARDSV
     SYRAYIAESK HLLPDSLLIK RMPIGQTDVI QKAQRERFAD FYNTWYRPDR ITVVAVGDFN
     PKSTIALINK EFGGIKARAP ARADYEFGKV TPPSGVDIGY HYDAEAPTTN ISIEALQPFP
     GLDKTQIRLN DVRMQLALDI VSRRLDILAH KDDAIISAGY VGVNDLMTET RVSSLEVTTK
     PENWQAALAL AEQQLRQAWQ YGFTADELRV AVANMRTSLQ QAADTARTRR SPQLAGALTD
     ALNDQNVFTS PQQDLALLTP LLNSITPEEA LTAFRGAWTG GRKLFVSGNV KLDDAQAQIN
     AAWKASTAAA VIAPAKDAAV EFPYTQFGNA PGKITAQKQV DDLAITQLTF ANGVRVNIKK
     TPYEANTIRI NARVGGGLLT EPAQKQPGLA YVADLAFRAG GLDKLSWDDL QTAMAGKQVG
     LEFGVGSDAL EFSARTNTEN LKLQLQLIAA YLTHAGYRPE ALSAARKAIA QNAISLEHTP
     EGMLRSRIPR ELASNDPRFG VPSRDEASAR TLAELKAWLD PQLQHGPLEI SLVGDLETPQ
     VIQALSETLG ALPARDAKPD YAEARKVKFP APLTETLKVS TQIDRGVVFM VWPTPDALDV
     TVNRRFNLLS EIMRNRLWDT IRTQMGSSYS PTAFSQMSDT FTHYGMLGVM ITVEPGAAPK
     VAEAVKGIAA ELQKTGISDD ELERARAPVL TDIRDSAQNN SYWLHVVLDG SQERPQRLDW
     ARTRLSGYEH ISKAEITAII KQYLKPEDVS TFIVLPVAQA K
//