ID A0A2A8CYH1_9BACT Unreviewed; 985 AA.
AC A0A2A8CYH1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:PEN13627.1};
GN ORFNames=CRI94_09985 {ECO:0000313|EMBL:PEN13627.1};
OS Longibacter salinarum.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salisaetaceae;
OC Longibacter.
OX NCBI_TaxID=1850348 {ECO:0000313|EMBL:PEN13627.1, ECO:0000313|Proteomes:UP000220102};
RN [1] {ECO:0000313|EMBL:PEN13627.1, ECO:0000313|Proteomes:UP000220102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 52045 {ECO:0000313|EMBL:PEN13627.1,
RC ECO:0000313|Proteomes:UP000220102};
RA Goh K.M., Shamsir M.S., Lim S.W.;
RT "Draft genome of Longibacter Salinarum.";
RL Submitted (OCT-2017) 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:PEN13627.1}.
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DR EMBL; PDEQ01000004; PEN13627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A8CYH1; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000220102; 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: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};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000220102};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..49
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 50..985
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013196489"
FT DOMAIN 82..225
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 242..419
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 720..896
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 985 AA; 109843 MW; F8A51A84193D1F88 CRC64;
MAAPLDGIHP HASSRPSILY MRSSLRSISR LALGAVLLML LAWSPFAQAQ QADADTSEEA
LPVDPAVRTG TLDNGMRFYI RQNDEPEDRL QLRLALNAGS ILETDAQRGL AHFLEHMLFN
GTENFEEQKL IDFLERTGME FGPDVNAYTS FDETVYKLRV PTDSLELVKT SFMVLRDWAS
RATLSEEEID KERGVVIEEW RQSQETAQGR MQDDIVSTLF AGSRYADRLP IGDTSVVKNA
PYSEVRDYYE TWYRPDLMAI IAVGDMDPDM LETMIRDRFS DFESPSDPQE RKRYDVPAHE
DTKYAVVTDP EYPVSSVATI FKTDAQPVRS KADFRRMLKE RLFFSMLNAR LSEKAQSGDA
PFLGAGGFNF TLARPMKGYG LQAQVPEDSI VAGMEALLTE ATRIRQHGFT DSELIRQKRD
LLRSYETSYN ERENIPSQSL AQQYVQLFLT GESAPGIETE YELAKEIMPT ITLADVNAVT
STIVADRNRA VLVQMPEKEG LEPPSEDTLA AVLDRVRTKD VEPYEDEMSD VPLMADIPEP
AGLKSTETID TLGTTVWTLE NGVTVVHKPT EFKDDEIRFT ATSPGGASTI SDDAYRSMRF
APNVVRQSGV GPFDNTALKK YLQGKSVSVS PYISSRDEGM NGSASPQDLE TMFQLIHSYA
TAPRIDANAL QSFKQQLTAR LKNRSATPTA ALQDTLVAKV YDNHPRVSPP EIAEVEALIA
DSLLGYYRTR FADASDFTFT FAGNVPTDSL AQFARTYLGT LPTIERTDEV RAVTPAPPND
VVEAEVRAGQ GQRSIVLLTY NGDIEYTREN RHALTTLSDV LSIKLREELR EKRGGTYNVG
VRDNTTGPPY NRYSFTVSFV CDPDRAADLL AAAKAEIDSV RTGGVTADDI AKVQEQQRRS
RETAMETNSF WVSALDQAFT TESVEPLDIY RYEELVSSST PETVAQTAQS YLNENRYYQV
VLYPEDFEAN AETSDGEAST EAGEK
//