ID Q0AAB6_ALKEH Unreviewed; 427 AA.
AC Q0AAB6;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 94.
DE SubName: Full=Peptidase M48, Ste24p {ECO:0000313|EMBL:ABI56221.1};
GN OrderedLocusNames=Mlg_0867 {ECO:0000313|EMBL:ABI56221.1};
OS Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Alkalilimnicola.
OX NCBI_TaxID=187272 {ECO:0000313|EMBL:ABI56221.1, ECO:0000313|Proteomes:UP000001962};
RN [1] {ECO:0000313|Proteomes:UP000001962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1
RC {ECO:0000313|Proteomes:UP000001962};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S.,
RA Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B.,
RA Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.;
RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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DR EMBL; CP000453; ABI56221.1; -; Genomic_DNA.
DR RefSeq; WP_011628616.1; NC_008340.1.
DR AlphaFoldDB; Q0AAB6; -.
DR KEGG; aeh:Mlg_0867; -.
DR eggNOG; COG4783; Bacteria.
DR HOGENOM; CLU_039394_0_0_6; -.
DR OMA; HEIVHAA; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000001962; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07333; M48C_bepA_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF13432; TPR_16; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003983};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW Reference proteome {ECO:0000313|Proteomes:UP000001962};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..427
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004167972"
FT DOMAIN 64..248
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 427 AA; 47023 MW; E3102442066F0429 CRC64;
MRILNRIFVL VLLALVLTAC AANPVTGQRE LALLSEREEV AIGEQHYDTT QQSMGGPYTT
DEALNRYINR VGQSLAEVSD RPHLPYEFVV INDSTPNAWA LPGGKMGINR GLLLEMDSEA
ELAAVLGHEI VHAAARHGAQ RVERGLLLQA GIMAVGIGAS AADRDIGPLL VAGAGIGATL
IMQRYSRHHE LEADRFGMEY MARAGYDPQG AVDLMETFLR MHDRGDPSWL EGLFASHPPS
RERLEANRQT VRELQSRCGE CRMGREAYQQ AIAGLRERQE AFEAHDRARE ALRAGNTAEA
MRLADQAVQR YPDEAIFHGL RGDILSVRGQ HGQAVRAYDR ALVRNSEYFA FHLGRGMAHN
ELGNHSQARR DLERSNDLLP NAVAHNALGK LALAAGDTDR ARGHFTVAAQ SNSPEGREAQ
ARLQRLQ
//