ADCA_STRR6
ID ADCA_STRR6 Reviewed; 501 AA.
AC Q8CWN2;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Zinc-binding lipoprotein AdcA;
DE Flags: Precursor;
GN Name=adcA; OrderedLocusNames=spr1975;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-423.
RX PubMed=9765793; DOI=10.1016/s0923-2508(97)87643-7;
RA Dintilhac A., Claverys J.-P.;
RT "The adc locus, which affects competence for genetic transformation in
RT Streptococcus pneumoniae, encodes an ABC transporter with a putative
RT lipoprotein homologous to a family of streptococcal adhesins.";
RL Res. Microbiol. 148:119-131(1997).
RN [3]
RP SEQUENCE REVISION.
RA Claverys J.-P.;
RT "Reevaluation of the size of the Zn-binding lipoprotein AdcA and evidence
RT for two domains.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=9379902; DOI=10.1046/j.1365-2958.1997.5111879.x;
RA Dintilhac A., Alloing G., Granadel C., Claverys J.-P.;
RT "Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants
RT exhibit a requirement for Zn and Mn resulting from inactivation of putative
RT ABC metal permeases.";
RL Mol. Microbiol. 25:727-739(1997).
CC -!- FUNCTION: Part of the ATP-driven transport system AdcABC for zinc.
CC Required for transformability. {ECO:0000269|PubMed:9379902}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC {ECO:0000305}.
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DR EMBL; AE007317; AAL00777.1; -; Genomic_DNA.
DR EMBL; Z71552; CAA96185.1; -; Genomic_DNA.
DR PIR; D98118; D98118.
DR RefSeq; NP_359566.1; NC_003098.1.
DR RefSeq; WP_000724074.1; NC_003098.1.
DR PDB; 7JJ8; X-ray; 2.03 A; A/B/C/D=27-325.
DR PDB; 7JJ9; X-ray; 1.58 A; A=27-501.
DR PDB; 7JJA; X-ray; 1.01 A; A=321-501.
DR PDB; 7JJB; X-ray; 1.10 A; A=321-501.
DR PDBsum; 7JJ8; -.
DR PDBsum; 7JJ9; -.
DR PDBsum; 7JJA; -.
DR PDBsum; 7JJB; -.
DR AlphaFoldDB; Q8CWN2; -.
DR SMR; Q8CWN2; -.
DR STRING; 171101.spr1975; -.
DR EnsemblBacteria; AAL00777; AAL00777; spr1975.
DR GeneID; 60234009; -.
DR KEGG; spr:spr1975; -.
DR PATRIC; fig|171101.6.peg.2138; -.
DR eggNOG; COG0803; Bacteria.
DR eggNOG; COG3443; Bacteria.
DR HOGENOM; CLU_016838_7_0_9; -.
DR OMA; ETWVPKV; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR GO; GO:0006829; P:zinc ion transport; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR006129; AdhesinB.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR006128; Lipoprotein_4.
DR InterPro; IPR015304; ZinT_dom.
DR InterPro; IPR006127; ZnuA-like.
DR Pfam; PF09223; ZinT; 1.
DR Pfam; PF01297; ZnuA; 1.
DR PRINTS; PR00691; ADHESINB.
DR PRINTS; PR00690; ADHESNFAMILY.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Competence; Ion transport; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Signal; Transport; Zinc;
KW Zinc transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT CHAIN 19..501
FT /note="Zinc-binding lipoprotein AdcA"
FT /id="PRO_0000031867"
FT REGION 116..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="S -> T (in Ref. 2; CAA96185)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="Q -> E (in Ref. 2; CAA96185)"
FT /evidence="ECO:0000305"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:7JJ9"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:7JJ9"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:7JJ9"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:7JJ9"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:7JJ9"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:7JJ9"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:7JJ9"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:7JJ9"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:7JJ9"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:7JJ9"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:7JJ9"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:7JJ9"
FT HELIX 145..162
FT /evidence="ECO:0007829|PDB:7JJ9"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:7JJ9"
FT HELIX 167..192
FT /evidence="ECO:0007829|PDB:7JJ9"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:7JJ9"
FT HELIX 208..214
FT /evidence="ECO:0007829|PDB:7JJ9"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:7JJ9"
FT HELIX 232..245
FT /evidence="ECO:0007829|PDB:7JJ9"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:7JJ9"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:7JJ9"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:7JJ9"
FT HELIX 283..287
FT /evidence="ECO:0007829|PDB:7JJ9"
FT HELIX 292..307
FT /evidence="ECO:0007829|PDB:7JJ9"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:7JJA"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:7JJA"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:7JJA"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:7JJA"
FT HELIX 351..355
FT /evidence="ECO:0007829|PDB:7JJA"
FT TURN 356..359
FT /evidence="ECO:0007829|PDB:7JJA"
FT HELIX 360..370
FT /evidence="ECO:0007829|PDB:7JJA"
FT HELIX 375..386
FT /evidence="ECO:0007829|PDB:7JJA"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:7JJA"
FT STRAND 397..404
FT /evidence="ECO:0007829|PDB:7JJA"
FT STRAND 407..422
FT /evidence="ECO:0007829|PDB:7JJA"
FT STRAND 428..436
FT /evidence="ECO:0007829|PDB:7JJA"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:7JJA"
FT STRAND 445..450
FT /evidence="ECO:0007829|PDB:7JJA"
FT STRAND 460..469
FT /evidence="ECO:0007829|PDB:7JJA"
FT HELIX 471..474
FT /evidence="ECO:0007829|PDB:7JJA"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:7JJA"
FT HELIX 491..499
FT /evidence="ECO:0007829|PDB:7JJA"
SQ SEQUENCE 501 AA; 56272 MW; 4677A2DE6CEE678A CRC64;
MKKISLLLAS LCALFLVACS NQKQADGKLN IVTTFYPVYE FTKQVAGDTA NVELLIGAGT
EPHEYEPSAK AVAKIQDADT FVYENENMET WVPKLLDTLD KKKVKTIKAT GDMLLLPGGE
EEEGDHDHGE EGHHHEFDPH VWLSPVRAIK LVEHIRDSLS ADYPDKKETF EKNAAAYIEK
LQSLDKAYAE GLSQAKQKSF VTQHAAFNYL ALDYGLKQVA ISGLSPDAEP SAARLAELTE
YVKKNKIAYI YFEENASQAL ANTLSKEAGV KTDVLNPLES LTEEDTKAGE NYISVMEKNL
KALKQTTDQE GPAIEPEKAE DTKTVQNGYF EDAAVKDRTL SDYAGNWQSV YPFLEDGTFD
QVFDYKAKLT GKMTQAEYKA YYTKGYQTDV TKINITDNTM EFVQGGQSKK YTYKYVGKKI
LTYKKGNRGV RFLFEATDAD AGQFKYVQFS DHNIAPVKAE HFHIFFGGTS QETLFEEMDN
WPTYYPDNLS GQEIAQEMLA H
