OMPA_KLEPN
ID OMPA_KLEPN Reviewed; 344 AA.
AC P24017; O69435;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Outer membrane protein A {ECO:0000255|HAMAP-Rule:MF_00842};
DE AltName: Full=Outer membrane porin A {ECO:0000255|HAMAP-Rule:MF_00842};
DE AltName: Full=Outer membrane protein 3A {ECO:0000303|PubMed:1955870};
DE Flags: Precursor;
GN Name=ompA {ECO:0000255|HAMAP-Rule:MF_00842};
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RV 308;
RX PubMed=9524233; DOI=10.1016/s0378-1119(98)00060-2;
RA Nguyen T.N., Samuelson P., Sterky F., Merle-Poitte C., Robert A.,
RA Baussant T., Haeuw J.F., Uhlen M., Binz H., Stahl S.;
RT "Chromosomal sequencing using a PCR-based biotin-capture method allowed
RT isolation of the complete gene for the outer membrane protein A of
RT Klebsiella pneumoniae.";
RL Gene 210:93-101(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 93-335.
RC STRAIN=LD119;
RX PubMed=1955870; DOI=10.1099/00221287-137-8-1911;
RA Lawrence J.G., Ochman H., Hartl D.L.;
RT "Molecular and evolutionary relationships among enteric bacteria.";
RL J. Gen. Microbiol. 137:1911-1921(1991).
RN [3] {ECO:0007744|PDB:2K0L}
RP STRUCTURE BY NMR OF 1-207, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=18952100; DOI=10.1016/j.jmb.2008.10.021;
RA Renault M., Saurel O., Czaplicki J., Demange P., Gervais V., Lohr F.,
RA Reat V., Piotto M., Milon A.;
RT "Solution state NMR structure and dynamics of KpOmpA, a 210 residue
RT transmembrane domain possessing a high potential for immunological
RT applications.";
RL J. Mol. Biol. 385:117-130(2009).
RN [4] {ECO:0007744|PDB:5NHX}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 209-334.
RA Nars G., Iordanov I., Saurel O., Tranier S., Mourey L., Milon A.,
RA Demange P.;
RT "Structure and dynamics of the C-terminal domain of OmpA from Klebsiella
RT pneumonia.";
RL Submitted (MAR-2017) to the PDB data bank.
CC -!- FUNCTION: With TolR probably plays a role in maintaining the position
CC of the peptidoglycan cell wall in the periplasm. Acts as a porin with
CC low permeability that allows slow penetration of small solutes; an
CC internal gate slows down solute passage. {ECO:0000255|HAMAP-
CC Rule:MF_00842}.
CC -!- FUNCTION: Required for conjugation with F-type plasmids; probably
CC serves as the mating receptor on recipient cells. {ECO:0000255|HAMAP-
CC Rule:MF_00842}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000255|HAMAP-Rule:MF_00842}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00842, ECO:0000305|PubMed:18952100}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00842, ECO:0000269|PubMed:18952100}.
CC -!- DOMAIN: The extracellular loops are most variable in sequence, and in
CC some bacteria confer sensitivity to phage and/or colicins.
CC {ECO:0000255|HAMAP-Rule:MF_00842}.
CC -!- SIMILARITY: Belongs to the outer membrane OOP (TC 1.B.6) superfamily.
CC OmpA family. {ECO:0000255|HAMAP-Rule:MF_00842}.
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DR EMBL; AJ000998; CAA04450.1; -; Genomic_DNA.
DR EMBL; M63355; AAA25119.1; -; Genomic_DNA.
DR PDB; 2K0L; NMR; -; A=1-207.
DR PDB; 5NHX; X-ray; 1.95 A; A=209-334.
DR PDBsum; 2K0L; -.
DR PDBsum; 5NHX; -.
DR AlphaFoldDB; P24017; -.
DR BMRB; P24017; -.
DR SMR; P24017; -.
DR TCDB; 1.B.6.1.11; the ompa-ompf porin (oop) family.
DR EvolutionaryTrace; P24017; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034220; P:ion transmembrane transport; IEA:UniProtKB-UniRule.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 3.30.1330.60; -; 1.
DR HAMAP; MF_00842; OmpA; 1.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR InterPro; IPR006664; OMP_bac.
DR InterPro; IPR002368; OmpA.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR006690; OMPA-like_CS.
DR InterPro; IPR036737; OmpA-like_sf.
DR InterPro; IPR000498; OmpA-like_TM_dom.
DR Pfam; PF00691; OmpA; 1.
DR Pfam; PF01389; OmpA_membrane; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR PRINTS; PR01022; OUTRMMBRANEA.
DR SUPFAM; SSF103088; SSF103088; 1.
DR SUPFAM; SSF56925; SSF56925; 1.
DR PROSITE; PS01068; OMPA_1; 1.
DR PROSITE; PS51123; OMPA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Conjugation; Disulfide bond;
KW Ion transport; Membrane; Porin; Repeat; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..?
FT /evidence="ECO:0000305"
FT CHAIN ?..344
FT /note="Outer membrane protein A"
FT /id="PRO_0000020097"
FT TOPO_DOM 1..14
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:18952100"
FT TRANSMEM 15..24
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18952100"
FT TOPO_DOM 25..49
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:18952100"
FT TRANSMEM 50..59
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18952100"
FT TOPO_DOM 60..62
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:18952100"
FT TRANSMEM 63..71
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18952100"
FT TOPO_DOM 72..89
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:18952100"
FT TRANSMEM 90..100
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18952100"
FT TOPO_DOM 101..104
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:18952100"
FT TRANSMEM 105..114
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18952100"
FT TOPO_DOM 115..139
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:18952100"
FT TRANSMEM 140..149
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18952100"
FT TOPO_DOM 150..153
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:18952100"
FT TRANSMEM 154..162
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:18952100"
FT TOPO_DOM 163..179
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:18952100"
FT TRANSMEM 180..188
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:18952100"
FT TOPO_DOM 189..344
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:18952100"
FT REPEAT 199..200
FT /note="1"
FT REPEAT 201..202
FT /note="2"
FT REPEAT 203..204
FT /note="3"
FT REPEAT 205..206
FT /note="4"
FT DOMAIN 208..336
FT /note="OmpA-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT REGION 199..206
FT /note="4 X 2 AA tandem repeats of A-P"
FT SITE 66
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT SITE 157
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT DISULFID 309..321
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT CONFLICT 335
FT /note="Y -> I (in Ref. 2; AAA25119)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:2K0L"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:2K0L"
FT STRAND 50..60
FT /evidence="ECO:0007829|PDB:2K0L"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:2K0L"
FT STRAND 90..117
FT /evidence="ECO:0007829|PDB:2K0L"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2K0L"
FT STRAND 136..149
FT /evidence="ECO:0007829|PDB:2K0L"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2K0L"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:2K0L"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:2K0L"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:2K0L"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:5NHX"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:5NHX"
FT HELIX 230..244
FT /evidence="ECO:0007829|PDB:5NHX"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:5NHX"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:5NHX"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:5NHX"
FT HELIX 265..286
FT /evidence="ECO:0007829|PDB:5NHX"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:5NHX"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:5NHX"
FT TURN 306..311
FT /evidence="ECO:0007829|PDB:5NHX"
FT HELIX 315..321
FT /evidence="ECO:0007829|PDB:5NHX"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:5NHX"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:5NHX"
SQ SEQUENCE 344 AA; 37061 MW; AC88AAE3B7871B16 CRC64;
MKAIFVLNAA PKDNTWYAGG KLGWSQYHDT GFYGNGFQNN NGPTRNDQLG AGAFGGYQVN
PYLGFEMGYD WLGRMAYKGS VDNGAFKAQG VQLTAKLGYP ITDDLDIYTR LGGMVWRADS
KGNYASTGVS RSEHDTGVSP VFAGGVEWAV TRDIATRLEY QWVNNIGDAG TVGTRPDNGM
LSLGVSYRFG QEDAAPVVAP APAPAPEVAT KHFTLKSDVL FNFNKATLKP EGQQALDQLY
TQLSNMDPKD GSAVVLGYTD RIGSEAYNQQ LSEKRAQSVV DYLVAKGIPA GKISARGMGE
SNPVTGNTCD NVKARAALID CLAPDRRVEI EVKGYKEVVT QPQA
