ID A0A0K6H1Q0_9GAMM Unreviewed; 928 AA.
AC A0A0K6H1Q0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Predicted Zn-dependent peptidase {ECO:0000313|EMBL:CUA84907.1};
GN ORFNames=Ga0061064_1046 {ECO:0000313|EMBL:CUA84907.1};
OS Pseudidiomarina woesei.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=1381080 {ECO:0000313|EMBL:CUA84907.1, ECO:0000313|Proteomes:UP000182598};
RN [1] {ECO:0000313|Proteomes:UP000182598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27808 {ECO:0000313|Proteomes:UP000182598};
RA Varghese N.;
RL Submitted (AUG-2015) 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; CYHB01000002; CUA84907.1; -; Genomic_DNA.
DR RefSeq; WP_055438711.1; NZ_LIPW01000002.1.
DR AlphaFoldDB; A0A0K6H1Q0; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000182598; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..928
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005503930"
FT DOMAIN 57..195
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 215..388
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 500..621
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 655..835
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 928 AA; 101307 MW; 08FCEF774525FFB9 CRC64;
MKFRHTLTAV AVASVLLTGC QATANNAPAT ETTAVAAQQF PNVAINYESF TLDNGLRVVV
HEDRKAPIVA VNVWYAVGSK DEKQGQTGFA HLFEHLMFNG TENYDDEYFG PFERAGATDM
NGTTNSDRTN YFQNVPTPAL DMALWMESDR MGHLLGAVTQ AKLDEQRGVV QNEKRQGEAQ
PYGRVFGFLA EQTFPEGHPY SWSTIGSMED LNAASLEDVH QWFNDYYGAA NAVVVLAGDI
DVATAKEKMQ KYFGHIAPGK PLQKLESWVA KRTGTKRATM EDNVPAARVY KLWNTAEMGT
TDSTYLNLLT SILASGKNSR LYQRLVHEEQ IASMVSGFQY ERTLAGQFFV IADAKPGVEL
ERIEAIIDEE LAKIIAEGPT AEELARVKFS GVADFVRGAE RIGGFGGKSD LLAAGEVYHG
DPGFYKAEFE QLKSATPADI QAAAKRWLSD GAFVLNVVPQ PRYQPAAAQA DRSKLPEVGE
LPKLDLPELT TFTLSNGLEV ALAERHDVPT VQMNLSFDSG YASDFGGKVG TASFAMSMLR
EGTAQRTSQD IARELEMLGT NLYTNAGIDS STVSMDSLVA NLEPSLAIFA DVVQNAAFAE
DEIERKRGNW LENIKKEKAS PTSQAIRILP GLIFGDNHAY GVPLTGSGTE ASITSLTRDD
LISYRNTWLR PDNARLVIVG ATTEAEIKPM LEAALSNWQA PATAKPTKQF TDVAMQPQQR
VYIIDQPGAP QSTILAGHLA PSERVDNAEA LDVTNTILGG SFTSRINMNL REDKGWSYGA
RTIWSSYNEA GMFITMAPVQ TDKTKESIQE IVKELTQYQT KKPATAAELE KVQMNKTAKL
PGAYETKGAL LSAIVGTLDK GKDMAWLENY AERVTSITLD DVKANANTLI NPESLTWVII
GDAATITDEV RSLNLGEVTM LDSDGNPL
//