ID A0A2I8DDQ0_9BURK Unreviewed; 450 AA.
AC A0A2I8DDQ0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptidase M48 domain-containing protein {ECO:0000259|Pfam:PF01435};
GN ORFNames=C2U31_02175 {ECO:0000313|EMBL:AUT44874.1};
OS Achromobacter sp. AONIH1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1758194 {ECO:0000313|EMBL:AUT44874.1, ECO:0000313|Proteomes:UP000236176};
RN [1] {ECO:0000313|Proteomes:UP000236176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AONIH1 {ECO:0000313|Proteomes:UP000236176};
RX PubMed=29437920;
RG NISC Comparative Sequencing Program;
RA Weingarten R.A., Johnson R.C., Conlan S., Ramsburg A.M., Dekker J.P.,
RA Lau A.F., Khil P., Odom R.T., Deming C., Park M., Thomas P.J.,
RA Henderson D.K., Palmore T.N., Segre J.A., Frank K.M.;
RT "Genomic Analysis of Hospital Plumbing Reveals Diverse Reservoir of
RT Bacterial Plasmids Conferring Carbapenem Resistance.";
RL MBio 9:e02011-e02017(2018).
RN [2] {ECO:0000313|Proteomes:UP000236176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AONIH1 {ECO:0000313|Proteomes:UP000236176};
RA Segre J.A., Mullikin J.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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; CP026124; AUT44874.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I8DDQ0; -.
DR KEGG; achr:C2U31_02175; -.
DR OrthoDB; 5295941at2; -.
DR Proteomes; UP000236176; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; cd07328; M48_Ste24p_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR PANTHER; PTHR43221:SF1; PROTEASE HTPX; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000236176};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 50..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 183..418
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 450 AA; 49307 MW; 954A264771C835CE CRC64;
MVFVLGLGVP VAMAIIALWQ WQRVGALPTV PVTSLRYYGQ RSPWVHDALA LLAPLTLLLG
VLATASFCAA LVAIRRATAR AMQSRDALMQ AFENGRRWLP KFMLSQTVLV FGGLITLLSF
EAIIILSRPG VSDGGVKLGV FLAMVALALA WYGFKMLYGA LRQSERQGEP EPILLMGQSL
APHQAPRLWE FVREIAKRTD ARAPDAVVVG LNEGFFVTEH PVALVSGQPV PEGRVLYLPL
PYMAFLDRAQ VSAVIAHELG HFTGEDTGYS LRFAPIYRSF LDSIFAITNE HDEKDDGSRA
WVAAPVTLYG KWFLASFEEA MHHWSREREL AADAFGSRIA GTESSALALL RISGLHRIVD
AALAHNQQAP AEERGGVLKM VRRLVAEHGL DDPQERLQDQ QAHPLDSHPS LKQRLEALGV
AITPELLARA RDPRDAALLV ELGLESAVSA
//
