COPA_PSEUB
ID COPA_PSEUB Reviewed; 609 AA.
AC P12374;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Copper resistance protein A;
DE Flags: Precursor;
GN Name=copA;
OS Pseudomonas syringae pv. tomato.
OG Plasmid pPT23D.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=323;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PT23.2;
RX PubMed=3372485; DOI=10.1128/jb.170.6.2879-2883.1988;
RA Mellano M.A., Cooksey D.A.;
RT "Nucleotide sequence and organization of copper resistance genes from
RT Pseudomonas syringae pv. tomato.";
RL J. Bacteriol. 170:2879-2883(1988).
RN [2]
RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF 33-37.
RC STRAIN=PT23.2;
RX PubMed=1924351; DOI=10.1073/pnas.88.20.8915;
RA Cha J.-S., Cooksey D.A.;
RT "Copper resistance in Pseudomonas syringae mediated by periplasmic and
RT outer membrane proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8915-8919(1991).
CC -!- FUNCTION: Mediates copper resistance by sequestration of copper in the
CC periplasm along with the copper-binding protein CopC. May have oxidase
CC activity.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: By copper.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. CopA subfamily.
CC {ECO:0000305}.
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DR EMBL; M19930; AAA25806.1; -; Genomic_DNA.
DR PIR; A32018; KSPSCY.
DR RefSeq; WP_054090693.1; NZ_SNVE01000046.1.
DR AlphaFoldDB; P12374; -.
DR SMR; P12374; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd13848; CuRO_1_CopA; 1.
DR CDD; cd13874; CuRO_2_CopA; 1.
DR CDD; cd13896; CuRO_3_CopA; 1.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR006376; Cu-R_CopA.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034284; CuRO_1_CopA.
DR InterPro; IPR034282; CuRO_2_CopA.
DR InterPro; IPR034279; CuRO_3_CopA.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR TIGRFAMs; TIGR01480; copper_res_A; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Metal-binding; Oxidoreductase;
KW Periplasm; Plasmid; Repeat; Signal.
FT SIGNAL 1..32
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:1924351"
FT CHAIN 33..609
FT /note="Copper resistance protein A"
FT /id="PRO_0000002949"
FT REPEAT 367..374
FT /note="1"
FT REPEAT 375..382
FT /note="2"
FT REPEAT 408..415
FT /note="3"
FT REPEAT 419..426
FT /note="4"
FT REPEAT 427..434
FT /note="5"
FT REGION 367..434
FT /note="5 X 8 AA tandem repeats of D-H-X-X-M-X-G-M"
FT BINDING 100
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 542
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000255"
FT BINDING 545
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000255"
FT BINDING 547
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000255"
FT BINDING 590
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000255"
FT BINDING 591
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000255"
FT BINDING 592
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000255"
FT BINDING 596
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000255"
FT BINDING 601
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000255"
SQ SEQUENCE 609 AA; 67355 MW; 9C086528E8135252 CRC64;
MESRTSRRTF VKGLAAAGVL GGLGLWRSPS WAASGSPALS VLSGTEFDLS IGEMPVNITG
RRRTAMAING GLPGPLLRWK EGDTVTLRVR NRLDAATSIH WHGIILPPNM DGVPGLSFAG
IEPGGVYVYQ FKVQQNGTYW YHSHSGFQEQ VGVYGPLVIE AKEPEPFKYD SEHVVMLTDW
TDEDPVSLMR TLKKQSDYYN FHKRTVGDFV NDVADKGWAA TVADRKMWAE MKMNPTDLAD
VSGATYTYLL NGQAPNMNWT GLFRPGEKLR LRFINGSAMT YFDIRIPGLK MTVVASDGQF
VNPVEVDELR IAVAETFDVI VEPTAEAYTV FAQSMDRTGY ARGTLAVREG LVAQVPPLDP
RPLVTMDDMG MGGMDHGSMD GMSGMDSGAD DGMQTMSSMG GDSMPAMDHS KMSTMQGMDH
GAMSGMDHGA MGGMVMQSHP ASENDNPLVD MQAMSPTAKL NDPGLGLRNN GRKVLTYADL
KSTFEDPDGR EPSRTIELHL TGHMEKFAWS FDGIKFADAQ PLILKYGERV RIVLVNDTMM
THPIHLHGMW SDLEDEDGNF RVRKHTIDMP PGSKRSYRVT ADALGRWAYH CHLLYHMEMG
MFREVRVEE
