ID A0A498DIP8_9PROT Unreviewed; 643 AA.
AC A0A498DIP8;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Peptidase M48 {ECO:0000313|EMBL:RLL55990.1};
GN ORFNames=D8Y20_00685 {ECO:0000313|EMBL:RLL55990.1};
OS Mariprofundus sp. EBB-1.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=2650971 {ECO:0000313|EMBL:RLL55990.1, ECO:0000313|Proteomes:UP000270267};
RN [1] {ECO:0000313|Proteomes:UP000270267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EBB-1 {ECO:0000313|Proteomes:UP000270267};
RA Lopez A., Barco R., Canela R., Emerson D., Tully B., Abuyen K.,
RA Broomell S., Albino D., Beraki S., Dingmon T., Estrada S., Fernandez M.,
RA Amend J.;
RT "Genome Sequence of Zetaproteobacterium sp. EBB-1: a novel, marine, iron-
RT oxidizing chemolithoautotroph isolated from an iron-sulfide mineral.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:RLL55990.1}.
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DR EMBL; RCFQ01000001; RLL55990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498DIP8; -.
DR Proteomes; UP000270267; Unassembled WGS sequence.
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; cd07340; M48B_Htpx_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR029024; TerB-like.
DR PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR PANTHER; PTHR43221:SF2; PROTEASE HTPX HOMOLOG; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR SUPFAM; SSF158682; TerB-like; 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:UP000270267};
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 17..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 115..333
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 643 AA; 70527 MW; 6AF9399CBB9A12A3 CRC64;
MKDFFGQQEQ AKRNTSFLVL MFVCAVILIV FSVYLAVTAG LLVTQVFIAQ QTDLFIHDFW
DVDRFLWING ITLMIVAAGS VYRTHQLKQG GGSAVAALLA AERVPSNSMD PLHSRLLNIV
EEMAIASGMP VPPVYLLSQS GINAFAAGFG PRDAVITVSQ GAVELLSRDE LQGVIAHEFS
HILNGDIALK MRLMGLLFGI TLISDCGIVM MTARGSSRHH GQERGTHPAM LVMGFMIFMV
GTIGSVFADM IKRAVSRQRE FLADAAAVQF TRNPEGIAGA LKVIGGYASG SRIQHAATQQ
TSHFFFCNAV KSWENKNWWA THPPLIERIK RLEPGFNGHV NSVDAVTRRA EVMSGAMHAF
DAGQGIATGL VASADALMLS IGKPDGEALQ HARHILNRMP KRVTDFAHDS FTARAVMYAL
LLDSASTIRK GQLNQLQKQA DASVFRELLD IQPLVAKLDP ELRIPLLEML IPALKSLSRT
QFDTFRGCIS SLIRADHKTD LFEYMLQRML LRHLYPSFLK TKPLKVCFDS PEQVIDQVAE
LIVLLIDRGR HVNPANTFKL AMSAFHEGDM PDMPVISAGV IHTLDEALKK LERSSPALKR
TLLKACVVTV LADGNTAIAE IELVRAIADA LDVPVPPFDT STQ
//
