ID   H1HMK1_9BACT            Unreviewed;       968 AA.
AC   H1HMK1;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Peptidase M16 inactive domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF9944_01395 {ECO:0000313|EMBL:EHO70188.1};
OS   Segatella maculosa OT 289.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=999422 {ECO:0000313|EMBL:EHO70188.1, ECO:0000313|Proteomes:UP000003167};
RN   [1] {ECO:0000313|EMBL:EHO70188.1, ECO:0000313|Proteomes:UP000003167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT 289 {ECO:0000313|EMBL:EHO70188.1,
RC   ECO:0000313|Proteomes:UP000003167};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA   Mathney J., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella maculosa OT 289.";
RL   Submitted (DEC-2011) 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:EHO70188.1}.
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DR   EMBL; AGEK01000027; EHO70188.1; -; Genomic_DNA.
DR   RefSeq; WP_008565355.1; NZ_JH594503.1.
DR   AlphaFoldDB; H1HMK1; -.
DR   STRING; 999422.HMPREF9944_01395; -.
DR   PATRIC; fig|999422.3.peg.1449; -.
DR   HOGENOM; CLU_306466_0_0_10; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000003167; 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:SF17; PROTEIN YHJJ; 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:UP000003167};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..968
FT                   /note="Peptidase M16 inactive domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003551569"
FT   DOMAIN          50..94
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          253..419
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          717..876
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   968 AA;  110475 MW;  46363F2FAC5598BF CRC64;
     MRRKTILFTL TLALTASVSA KDYHFTTVKG DAMQTRIYTL DNGLKVYMSV NKEKPRLQAN
     IAVRTGSRND PAETTGLAHY LEHLMFKGTQ QFGTTDYAKE KPYLDDIERR YEHYRTLTDP
     TMRKQAYHEI DSVSQLAAQY NIPNEYDKLM ASIGSEGSNA YTSNDVTCYV ENIPSNEIEN
     WARIQADRFR NMIIRGFHTE LEAVYEEKNI SMGSDGTKEY AALWKLLTPT HPYGTQTTIG
     EQEHLKNPSI VNIKNYFHRY YVPNNVAIAL AGDFDPDATI AVIDKYFGTW KAGKRLTRPE
     FPAQKAITMP RDTSVVGQDA ENVMMGWRFK GANQLQNDTL DIVRRMLSNG KAGLLDINID
     QQMKAMETGA FLDDLHDYSA LIIEGVPAHG QKLEDLRSLI LAEISKLGRG EFSDDLLPAV
     LANKKLQYFR SLDNNRSRVQ MMVDAFINDK KWAATALQID RQSRLTKQDI IGFARRHLRM
     DNFVCVYKRM GIDSTLKKIE KPIITPIPAN REFESPFLNA IRMAKTKPIR PVFVDYNKEL
     AQGKLSSGLP YIYKRNTDDG LFNLVFRYDF GSTADNRYGY AADYLNYIGT RDMTISQIKQ
     AFYKLACSYS VSVGERNISI SLSGLNENMP EALQLLEKVL HQSKADNDSW SRYCDLTKKS
     RADAKTDQKA NFNALWDYAV YGKYNPTRNI IATQALRSMD PQQLISLLDK LNGLKHTVLY
     YGPSDLKTLE AVIVSTHKTP QKLAAGPVNK LYEPQNTDNN EVLIAPYDAK NIYMRQYNNR
     GGEWSLARTP VETLFNQYFG GGMNSVVFQE LRETRGLAYN AYAVYKRPEY KGESESFFTH
     IISQNDKMND CIKVFHEILV SMPQNQAAFD LAKQSLRKSI QSSRTTKFGV IQRYLSLRQL
     GLNHDYMQDV YAALPRLTLK DIVNFANRNI AQESFRYAVL GDEKNLDMTL LEQIGPVQRL
     TTEDIFGY
//