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Database: UniProt
Entry: C1DAP9_LARHH
LinkDB: C1DAP9_LARHH
Original site: C1DAP9_LARHH 
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}.
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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
//
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