ID J1FDS9_9BACT Unreviewed; 483 AA.
AC J1FDS9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:EJF08379.1};
GN ORFNames=O71_21202 {ECO:0000313|EMBL:EJF08379.1};
OS Pontibacter sp. BAB1700.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1144253 {ECO:0000313|EMBL:EJF08379.1, ECO:0000313|Proteomes:UP000003746};
RN [1] {ECO:0000313|EMBL:EJF08379.1, ECO:0000313|Proteomes:UP000003746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB1700 {ECO:0000313|EMBL:EJF08379.1,
RC ECO:0000313|Proteomes:UP000003746};
RX PubMed=23105068; DOI=10.1128/JB.01550-12;
RA Joshi M.N., Sharma A.C., Pandya R.V., Patel R.P., Saiyed Z.M., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of Pontibacter sp. nov. BAB1700, a Halotolerant,
RT Industrially Important Bacterium.";
RL J. Bacteriol. 194:6329-6330(2012).
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:EJF08379.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKIS01000183; EJF08379.1; -; Genomic_DNA.
DR RefSeq; WP_007660029.1; NZ_AKIS01000183.1.
DR AlphaFoldDB; J1FDS9; -.
DR PATRIC; fig|1144253.3.peg.4185; -.
DR Proteomes; UP000003746; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
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:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
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 71..189
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 227..408
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 483 AA; 54329 MW; BACDA19EE4AE35CA CRC64;
MNHTPLQNYV KWGALALVLS LSACGQRTTT QSPEAATTTA ENVNTATENT APASAYQIPV
DYYTLDNGLK VVLSQDKTAP LATIAVYYNI GFRIEPKDRT GFAHLFEHMM FQGSENLGKM
EFIQLVQKNG GILNGSTRFD FTNYFEIVPA HKLETMLWAE ADRMKGLNIT QENLTNQQGV
VKNEVKVNVL NQPYGGFPWL DMPQYANKNW YNAHNFYGDL EDLDAASLED VQSFFDTYYS
PNNAVLVVVG DFETSEAKHW IQQYFAGIPS GDVPSLPDLS EPRQEKEQRF TKDDKLANRP
ALAFAYHMPE RNSPEYYAMG LLDQILLQGN DSRLYQALVQ ERGYASSVDG GINAFLGNMF
NYNGPMLWMG SLIHDQNVNA DEIVKVVDAE IQKLQQEGID QELIDLAIVK MRSSLYDQVS
ASSGFGKADL LATFALFDDD PSRINRLESE FRKVTPELLR KTIEEYLRPT NRTVLVVNPL
AKS
//
