ID A0A1H3NI62_9BURK Unreviewed; 915 AA.
AC A0A1H3NI62;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:SDY88370.1};
GN ORFNames=SAMN04515617_12711 {ECO:0000313|EMBL:SDY88370.1};
OS Collimonas sp. OK242.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=1798195 {ECO:0000313|EMBL:SDY88370.1, ECO:0000313|Proteomes:UP000198586};
RN [1] {ECO:0000313|EMBL:SDY88370.1, ECO:0000313|Proteomes:UP000198586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK242 {ECO:0000313|EMBL:SDY88370.1,
RC ECO:0000313|Proteomes:UP000198586};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; FNOR01000027; SDY88370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3NI62; -.
DR STRING; 1798195.SAMN04515617_12711; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000198586; 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; 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:SDY88370.1};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..915
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011719551"
FT DOMAIN 55..200
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 209..382
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 655..833
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 915 AA; 100609 MW; BFC2A587D8BAF808 CRC64;
MHLFRNRLLS CLLAAACGIG FIGITEAATA LPAGVTQGPS AEGITEYQFA NGFKVLLFPD
ASKPTVTVNM TYLVGSRFEN YGETGMAHLL EHLMFKGTPT HPSIPKDFSQ RGMSFNGTTN
VDRTNYYEIF QAGDDNLKWA IGMEADRMLH SFIARKDLDS EMTVVRNEYE QGENSPFGVL
IKRLEGVAYD WHNYGKPTIG NRSDIENVRI ENLQAFYKTY YQPDNAVLLI AGKFDPAKTL
AWVSQAFGKL PKPTRKMRDF WTVEPTQDGE RSVTVRRQGD VQIVAVAYKI PSELHPDSDA
LSYAGTILAD TPNGRLHKSL VETGKATAVF NYEMSGYAPG LEIIAAVVKK GEPIEPVRQA
LIDGVEQFAK TPPTPEEMER VRLANANSFE KLLNDHQRVG VAMSSTIALG DWRLLFLGRD
RSNKVTSAQV ATAAAHYFTR DNRTVGMFLP EDQLQRADVP AAPSVAGLLK DYEPQQAIAD
GEAFDPSQAN VDARTQRSQV GGLKLALLPK KTRGETVSVK LNLQWGDEKT LFGKKTASEL
ADAMLMRGSS TLTREQLADE FSKLKISGNL TQFQTTRSNL PAALKLVASV LKQPRFDPAE
FDRLRKESLV GLEASRNEPN TLAAEAIAQH FNKYPQGHWL AAQSVDQQIA AIQAATLADV
SAFHHDFYGA SQGELAIVGD FDVAAVSKVV QDEFGAWKSA APYQRVIRQN FDVAPLQKTI
NSPDKENGFY VARQNLDMRD DDADYPAMMV ANYLFGGGSL KSRLMDRVRQ KEGLSYGIGS
SVEISAISRA ARFSVQAIAA PQNLGKVDTA VKEELARALK EGFSADELAR AKSGILQENQ
RARAQDSALS AGWARLLDLN RTFAWSKQIE DKISALTVEQ VNQAFRKHIA PAQLSVVIVR
DEAKAKANTA MVAKP
//
