Y627_BARHE
ID Y627_BARHE Reviewed; 358 AA.
AC Q8VQ25; Q6G5C4;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Putative zinc metalloprotease BH06270;
DE EC=3.4.24.-;
GN OrderedLocusNames=BH06270;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zimmermann R., Augustin K., Schaal K., Sander A.;
RT "Cloning, nucleotide sequencing, and expression of a hemin-binding protein
RT of Bartonella henselae.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAF27431.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF461795; AAL66373.1; -; Genomic_DNA.
DR EMBL; BX897699; CAF27431.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011180551.1; NZ_LRIJ02000001.1.
DR AlphaFoldDB; Q8VQ25; -.
DR SMR; Q8VQ25; -.
DR STRING; 283166.BH06270; -.
DR PaxDb; Q8VQ25; -.
DR PRIDE; Q8VQ25; -.
DR EnsemblBacteria; CAF27431; CAF27431; BH06270.
DR GeneID; 64156906; -.
DR KEGG; bhe:BH06270; -.
DR eggNOG; COG0750; Bacteria.
DR Proteomes; UP000000421; Chromosome.
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: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 Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837; PTHR42837; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR TIGRFAMs; TIGR00054; TIGR00054; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..358
FT /note="Putative zinc metalloprotease BH06270"
FT /id="PRO_0000088430"
FT TRANSMEM 89..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 102..177
FT /note="PDZ"
FT ACT_SITE 8
FT /evidence="ECO:0000255"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT CONFLICT 321
FT /note="T -> S (in Ref. 1; AAL66373)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 39715 MW; AD99846E6FF1F704 CRC64;
MIIIFVHEAG HYLIGRWCGI KASVFSLGFG PQIVGYTDKR GTQWRLALIP LGGYVKFIGD
EEGLHGTSSQ SLPIVDGSFG SAHAWKKAAT VFAGPLFNVL FTVVILTFFF FTYGRVAIEP
VVGSFVKDSP AVQAGLQLGD RFIEMDGQQV ESFEDLMNYV TFHGGDPIEF KMERSGQVFT
TVITPKVVER DDGFGNRVRS GLMGVGVPVD PDNPARLDPA YVKHIRYSFG RALREASKRA
TFIVTQTVFF MGRLLGGKED HCRLSGPSKT VKIAWQVSET GFLSLLNFTA FLSIGVGLIN
LFPIPPLDGG YLLFHVVEII TGRPISAKIR EIIFRLGLCF VLLFMFFALF NDYFCWFS