ID C1DAP9_LARHH Unreviewed; 460 AA.
AC C1DAP9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:ACO73230.1};
GN OrderedLocusNames=LHK_00235 {ECO:0000313|EMBL:ACO73230.1};
OS Laribacter hongkongensis (strain HLHK9).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Laribacter.
OX NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO73230.1, ECO:0000313|Proteomes:UP000002010};
RN [1] {ECO:0000313|EMBL:ACO73230.1, ECO:0000313|Proteomes:UP000002010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLHK9 {ECO:0000313|EMBL:ACO73230.1,
RC ECO:0000313|Proteomes:UP000002010};
RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., Fan R.Y.,
RA Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., Huang J.D., Mak W.,
RA Pallen M.J., Lok S., Yuen K.Y.;
RT "The complete genome and proteome of Laribacter hongkongensis reveal
RT potential mechanisms for adaptations to different temperatures and
RT habitats.";
RL PLoS Genet. 5:E1000416-E1000416(2009).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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; CP001154; ACO73230.1; -; Genomic_DNA.
DR RefSeq; WP_012695725.1; NC_012559.1.
DR AlphaFoldDB; C1DAP9; -.
DR STRING; 557598.LHK_00235; -.
DR MEROPS; M16.019; -.
DR KEGG; lhk:LHK_00235; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_1_0_4; -.
DR Proteomes; UP000002010; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000002010};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..460
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002908382"
FT DOMAIN 38..173
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 190..372
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 460 AA; 50781 MW; 65ED005201E579FB CRC64;
MKAKWMGAMA ALAMASGSLA ASEPVTVEAT LENGMKVIVR PDRRAPVAVS QVWYRVGGLD
EVGVPTGLSH ALEHMMFKGT TTVADGEFSR RVAALGGREN AFTSKDYTAY FQQIGASHLP
EMFRLEADRM QNLKVDPQSL ARELEVIREE RRMRTDDNPG AMLMEAMGRH AFAGPSGQPV
IGWADDIPRI DAPVLKDWYQ RFYAPNNATL VVVGDVDPQA VLNEARATFG RLPARVVARP
QAVAEPDLPP GSQRFVLERP SELGYVALGW RVPRLAKPDE PDPYALEVLA AVLDGAAASR
LPRALVREQR LADSVSADYD MNGRGEQLFT VVAVPAAGQT PAALEQAVRR QLRQIADKGV
EPAELARVRQ QLRAGRVYER DSMFAQAMSM GAAESRGHSW RDEDEIDRRL AAVRSEDLQR
VVRRYFTDER LVVGELKPLP LTQAQRQASQ ASMKENPHVR
//