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Database: UniProt
Entry: A0A1Z1FBX7_9SPHN
LinkDB: A0A1Z1FBX7_9SPHN
Original site: A0A1Z1FBX7_9SPHN 
ID   A0A1Z1FBX7_9SPHN        Unreviewed;       227 AA.
AC   A0A1Z1FBX7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Site-2 protease family protein {ECO:0000313|EMBL:ARU16216.1};
GN   ORFNames=A9D14_08410 {ECO:0000313|EMBL:ARU16216.1};
OS   Croceicoccus marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceicoccus.
OX   NCBI_TaxID=450378 {ECO:0000313|EMBL:ARU16216.1, ECO:0000313|Proteomes:UP000195807};
RN   [1] {ECO:0000313|EMBL:ARU16216.1, ECO:0000313|Proteomes:UP000195807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E4A9 {ECO:0000313|EMBL:ARU16216.1,
RC   ECO:0000313|Proteomes:UP000195807};
RA   Wu Y.-H., Cheng H., Xu L., Huo Y.-Y., Wang C.-S., Xu X.-W.;
RT   "Complete genome sequence of esterase-producing bacterium Croceicoccus
RT   marinus E4A9.";
RL   Submitted (JAN-2017) 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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. 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}.
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DR   EMBL; CP019602; ARU16216.1; -; Genomic_DNA.
DR   RefSeq; WP_066845215.1; NZ_CP019602.1.
DR   AlphaFoldDB; A0A1Z1FBX7; -.
DR   STRING; 450378.GCA_001661675_01686; -.
DR   KEGG; cman:A9D14_08410; -.
DR   OrthoDB; 9800627at2; -.
DR   Proteomes; UP000195807; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06158; S2P-M50_like_1; 1.
DR   InterPro; IPR008915; Peptidase_M50.
DR   InterPro; IPR044537; S2P-M50-like.
DR   PANTHER; PTHR35864; ZINC METALLOPROTEASE MJ0611-RELATED; 1.
DR   PANTHER; PTHR35864:SF1; ZINC METALLOPROTEASE MJ0611-RELATED; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
PE   3: Inferred from homology;
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, ECO:0000313|EMBL:ARU16216.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195807};
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        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        52..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        95..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        178..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..188
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
SQ   SEQUENCE   227 AA;  24362 MW;  E7637E2682DCEA7D CRC64;
     MSDTIILAAI LIPCLIVAIV FHEVSHGWSA KMLGDPTAKE ARRLSLNPLR HVDPVGTVVL
     PGVMALIGGP VFGWAKPVPV NKWRLNNPRF GMMAVAAAGP GSNFVMAGIA AVVLGLLARG
     IDPGNVSAAM QWTITGIDYF ILINIFLAFF NLLPIPPFDG SHIVEGLLPR SAARAYEKLR
     PVGMLLLVAV IALSWFFPDL GIIENIVWPP VEWVRGLYIG LAEAIAS
//
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