ID A0A1Q9HFU8_9VIBR Unreviewed; 952 AA.
AC A0A1Q9HFU8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:OLQ88690.1};
GN ORFNames=BIY22_20900 {ECO:0000313|EMBL:OLQ88690.1};
OS Vibrio panuliri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1381081 {ECO:0000313|EMBL:OLQ88690.1, ECO:0000313|Proteomes:UP000186313};
RN [1] {ECO:0000313|EMBL:OLQ88690.1, ECO:0000313|Proteomes:UP000186313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 703 {ECO:0000313|EMBL:OLQ88690.1,
RC ECO:0000313|Proteomes:UP000186313};
RA Gonzalez-Castillo A., Gomez-Gil B., Enciso-Ibarra K.;
RT "Genomic Taxonomy of the Vibrionaceae.";
RL Submitted (SEP-2016) 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:OLQ88690.1}.
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DR EMBL; MJMJ01000021; OLQ88690.1; -; Genomic_DNA.
DR RefSeq; WP_075709041.1; NZ_MJMJ01000021.1.
DR AlphaFoldDB; A0A1Q9HFU8; -.
DR STRING; 1381081.BIY22_20900; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000186313; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 63..180
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 220..394
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 539..648
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 686..858
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 952 AA; 106192 MW; A41C2AF5063D3B43 CRC64;
MRKFLLGAVS LTALFGCTSN LDYSAPFFSS LPHGVKLVEE VDSVAGKATI PYSKYTLDNG
LTVILSPDHS DPLVHVDVTY HVGSAREDIG KSGFAHFFEH MMFQGSEHVG DQEHFRLITE
AGGSLNGTTN RDRTNYFETV PANQLEKMLW LESDRMGFLL DAVSQRKFEI QRDTVKNERA
QNYDNRPYGL MWERMGEAMY PEGHPYSWQT IGYIEDLNRV DVNDLKAFFL RWYGPNNAVL
TIGGDIDVDQ TLEWVSKYFG SIPRGPEVEQ APKQPATLNE DKYITLQDRI QQPMVLIGWP
TQYSGHQDEM ALNALASSLG SGANSLLYQK LVKTQKAVDA GAFQDCSELA CNFYIYAMAP
SGEKGQLKPL YQEMMQILNG FEQQGISQQR LDQITGMSES SAVFALQSVK GKVSQLAANQ
TFFGQPDRLQ SQLERIRAVT PESVMAAYKK YINGHHKVTL SVVPRGKLEM AVQPSNFTTP
KRTLPEYQPV KDGDLVYRRP VDSFDRSIMP QVAEAVQAEM PQLYRVYFDN GAELLGTVSD
ETPTVQLDIR LPAGERYAPS GKEGIANLTA AMMQEGTQQS TLEELQARLD KLGSSVSINA
GNYTTTISLA SLEKNLPQTL AIVNEVLFEP AFKEADFARV KKQMLEGMVY QHQQPSWLAS
QATRQVLFAG SIYQRPSDGS VESISNLTLQ DVKDFYHNQY TPQGAQIVVV GDLSKNDIVA
QLASIEAWQG DVPPLLSPQL VRPVSGQAIY LVDKPGAPQS VVRMVRQGLP FDATGEVYLT
QLANFNLAGN FNSRLNQNLR EEKGYTYGAS GYLASNREVG AVIFSAQVRA DATVPSIIEM
QKELQQYSEQ GMTDQELSFM RLAVGQQDAL KYETPSQKTQ LLGSILTFSL DEDYLQQRNK
IVETVNKDVL DALAKKWFNP EDYQIVVVGD AKKLKPQLES LQIPIKQLEI VQ
//
