ID A3VJM4_9RHOB Unreviewed; 352 AA.
AC A3VJM4;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
GN ORFNames=RB2654_04199 {ECO:0000313|EMBL:EAQ11601.1};
OS Maritimibacter alkaliphilus HTCC2654.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ11601.1, ECO:0000313|Proteomes:UP000002931};
RN [1] {ECO:0000313|EMBL:EAQ11601.1, ECO:0000313|Proteomes:UP000002931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ11601.1,
RC ECO:0000313|Proteomes:UP000002931};
RX PubMed=20729358; DOI=10.1128/JB.00873-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT genera.";
RL J. Bacteriol. 192:5552-5553(2010).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRNR:PIRNR006404,
CC ECO:0000256|PIRSR:PIRSR006404-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR006404,
CC ECO:0000256|PIRSR:PIRSR006404-2};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR006404};
CC Multi-pass membrane protein {ECO:0000256|PIRNR:PIRNR006404}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931, ECO:0000256|PIRNR:PIRNR006404}.
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:EAQ11601.1}.
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DR EMBL; AAMT01000014; EAQ11601.1; -; Genomic_DNA.
DR RefSeq; WP_008328945.1; NZ_VNHV01000005.1.
DR AlphaFoldDB; A3VJM4; -.
DR STRING; 314271.RB2654_04199; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG1994; Bacteria.
DR HOGENOM; CLU_037123_1_2_5; -.
DR OrthoDB; 9781963at2; -.
DR Proteomes; UP000002931; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02205; CBS_pair_SF; 1.
DR CDD; cd06164; S2P-M50_SpoIVFB_CBS; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR008915; Peptidase_M50.
DR InterPro; IPR016483; UCP006404_Pept_M50_CBS.
DR PANTHER; PTHR39188; MEMBRANE-ASSOCIATED ZINC METALLOPROTEASE M50B; 1.
DR PANTHER; PTHR39188:SF3; ZINC METALLOPROTEASE SLR1821-RELATED; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF02163; Peptidase_M50; 2.
DR PIRSF; PIRSF006404; UCP006404_Pept_M50_CBS; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122};
KW Cell membrane {ECO:0000256|PIRNR:PIRNR006404};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR006404};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR006404};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR006404};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|PIRNR:PIRNR006404};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR006404};
KW Reference proteome {ECO:0000313|Proteomes:UP000002931};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR006404};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|PIRNR:PIRNR006404};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006404}.
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 41..60
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 98..121
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 141..157
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 203..220
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT DOMAIN 47..120
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 141..189
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 300..350
FT /note="CBS"
FT /evidence="ECO:0000259|Pfam:PF00571"
FT ACT_SITE 59
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-1"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
SQ SEQUENCE 352 AA; 37654 MW; D1BB5D01C99ABDA7 CRC64;
MRWSFPIGRL LGSELRVHAT FLILLAYVGG SAYSFGGLDA ALVNVAYVLA LFACVIAHEY
GHALTARRFG IPTPDITLLP IGGVARLMRI PEKPGQEVLV ALAGPAVNVV IFFVLWITAG
LSFEAAPLTG GMTFADLPRE LATLNLILAA FNMIPAFPMD GGRVLRATLA MVTDRVKATR
IAAGVGQVLA VGFGIYGFYI GSFIYPIIAV FIFMAARAEA RDVRLRAMAK TETAGNVMAT
GFKALGTSLT LEQAREAFDR ERVAEFPVVD SASRRITGLL ARKQLDDQYH TLGAQAPITR
VMATNVPVVQ DGTPLAHVLR LLNSAPAVAV TDATGEVAGY ISHRTVMDRL GR
//
