(data stored in SCRATCH zone)

SWISSPROT: Q147A2_PARXL

ID   Q147A2_PARXL            Unreviewed;       296 AA.
AC   Q147A2;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 88.
DE   RecName: Full=Protease HtpX homolog {ECO:0000256|HAMAP-Rule:MF_00188};
DE            EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_00188};
GN   Name=htpX {ECO:0000256|HAMAP-Rule:MF_00188};
GN   ORFNames=Bxe_A4413 {ECO:0000313|EMBL:ABE28587.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28587.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28587.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28587.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00188};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00188};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00188}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00188}.
CC   -!- SIMILARITY: Belongs to the peptidase M48B family.
CC       {ECO:0000256|HAMAP-Rule:MF_00188, ECO:0000256|SAAS:SAAS00541274}.
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DR   EMBL; CP000270; ABE28587.1; -; Genomic_DNA.
DR   STRING; 266265.Bxe_A4413; -.
DR   MEROPS; M48.004; -.
DR   EnsemblBacteria; ABE28587; ABE28587; Bxe_A4413.
DR   KEGG; bxe:Bxe_A4413; -.
DR   eggNOG; ENOG4105D0M; Bacteria.
DR   eggNOG; COG0501; LUCA.
DR   HOGENOM; HOG000227301; -.
DR   KO; K03799; -.
DR   OMA; REYMADS; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00188; Pept_M48_protease_HtpX; 1.
DR   InterPro; IPR022919; Pept_M48_protease_HtpX.
DR   InterPro; IPR001915; Peptidase_M48.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q147A2.
DR   SWISS-2DPAGE; Q147A2.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00188};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00423899};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00112036};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00016464};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00473692};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00112271};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00473645};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Stress response {ECO:0000313|EMBL:ABE28587.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00016455};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00188,
KW   ECO:0000256|SAAS:SAAS00016434};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00188, ECO:0000256|SAAS:SAAS00473636}.
FT   TRANSMEM     12     36       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00188}.
FT   TRANSMEM     42     59       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00188}.
FT   TRANSMEM    152    176       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00188}.
FT   TRANSMEM    188    208       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00188}.
FT   DOMAIN       78    289       Peptidase_M48. {ECO:0000259|Pfam:
FT                                PF01435}.
FT   ACT_SITE    143    143       {ECO:0000256|HAMAP-Rule:MF_00188}.
FT   METAL       142    142       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00188}.
FT   METAL       146    146       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00188}.
FT   METAL       213    213       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00188}.
SQ   SEQUENCE   296 AA;  31856 MW;  E84A5525DEFEDACF CRC64;
     MNPALGQGVA DMFNWVKTAM LMAAITALFI VIGGMIGGSR GMTIALVIAL GMNFFSYWFS
     DKMVLRMYNA QEVDETSAPQ FYRMVRELST RAGLPMPRVY LINEDAPNAF ATGRNPEHAA
     VAATTGILRV LSEREMRGVM AHELAHVKHR DILISTVSAT MAGAISALAN FAMFFGGRDE
     NGRPTNPIAS IAVALLAPIA GALIQMAISR AREFEADRGG AQISGDPQAL ASALDKIHRY
     ASGIPFPTAE QHPATAQMMI MNPLAGGGIA NLFSTHPATE ERIARLMEMA RTGRFE
//

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