OMP38_ACIB2
ID OMP38_ACIB2 Reviewed; 356 AA.
AC Q6RYW5; D0CDF2;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Outer membrane protein Omp38 {ECO:0000303|PubMed:16008580};
DE AltName: Full=Outer membrane protein OmpA {ECO:0000303|PubMed:21965596};
DE Short=AbOmpA {ECO:0000303|PubMed:21965596};
DE AltName: Full=Outer membrane protein OmpAb {ECO:0000303|PubMed:9928952};
DE Flags: Precursor;
GN Name=omp38 {ECO:0000303|PubMed:16008580};
GN Synonyms=ompA {ECO:0000303|PubMed:21965596}; ORFNames=HMPREF0010_02782;
OS Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / JCM 6841 / CCUG
OS 19606 / CIP 70.34 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=575584;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN APOPTOSIS, SUBCELLULAR
RP LOCATION IN HOST CELLS, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC
RC 109757 / NCIMB 12457 / NCTC 12156 / 81;
RX PubMed=16008580; DOI=10.1111/j.1462-5822.2005.00538.x;
RA Choi C.H., Lee E.Y., Lee Y.C., Park T.I., Kim H.J., Hyun S.H., Kim S.A.,
RA Lee S.K., Lee J.C.;
RT "Outer membrane protein 38 of Acinetobacter baumannii localizes to the
RT mitochondria and induces apoptosis of epithelial cells.";
RL Cell. Microbiol. 7:1127-1138(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC
RC 109757 / NCIMB 12457 / NCTC 12156 / 81;
RX PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA Seifert H., Dijkshoorn L.;
RT "The success of Acinetobacter species; genetic, metabolic and virulence
RT attributes.";
RL PLoS ONE 7:E46984-E46984(2012).
RN [3]
RP FUNCTION AS A PORIN, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC
RC 109757 / NCIMB 12457 / NCTC 12156 / 81;
RX PubMed=9928952; DOI=10.1016/s0014-5793(98)01679-2;
RA Jyothisri K., Deepak V., Rajeswari M.R.;
RT "Purification and characterization of a major 40 kDa outer membrane protein
RT of Acinetobacter baumannii.";
RL FEBS Lett. 443:57-60(1999).
RN [4] {ECO:0007744|PDB:3TD3, ECO:0007744|PDB:3TD4, ECO:0007744|PDB:3TD5}
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 221-339 IN COMPLEX WITH
RP DIAMINOPIMELATE AND SYNTHETIC PEPTIDOGLYCAN, PEPTIDOGLYCAN-BINDING, DOMAIN,
RP AND MUTAGENESIS OF ASP-271 AND ARG-286.
RX PubMed=21965596; DOI=10.1096/fj.11-188425;
RA Park J.S., Lee W.C., Yeo K.J., Ryu K.S., Kumarasiri M., Hesek D., Lee M.,
RA Mobashery S., Song J.H., Kim S.I., Lee J.C., Cheong C., Jeon Y.H.,
RA Kim H.Y.;
RT "Mechanism of anchoring of OmpA protein to the cell wall peptidoglycan of
RT the gram-negative bacterial outer membrane.";
RL FASEB J. 26:219-228(2012).
RN [5] {ECO:0007744|PDB:4G4Y, ECO:0007744|PDB:4G4Z, ECO:0007744|PDB:4G88}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 221-339.
RA Lee W.C., Park J.S., Song J.H., Kim S.I., Lee J.C., Cheong J., Kim H.Y.;
RT "Enantiomer-dependent amino acid binding affinity of OmpA-like domains from
RT Acinetobacter baumannii peptidoglycan-associated lipoprotein and OmpA.";
RL Submitted (JUL-2012) to the PDB data bank.
CC -!- FUNCTION: Functions as a porin (PubMed:9928952). Induces apoptosis in
CC human cell lines through caspase-dependent and AIF-dependent pathways.
CC Purified Omp38 enters host cell and localizes to the mitochondria,
CC which presumably leads to a release of proapoptotic molecules such as
CC cytochrome c and AIF (apoptosis-inducing factor) (PubMed:16008580).
CC Binds peptidoglycan, contributes to cell wall maintenance (Probable).
CC {ECO:0000269|PubMed:16008580, ECO:0000269|PubMed:9928952,
CC ECO:0000305|PubMed:16008580, ECO:0000305|PubMed:21965596}.
CC -!- SUBUNIT: Homotrimer (PubMed:9928952). Forms a pore with a size of 1.3
CC nm (PubMed:9928952). {ECO:0000269|PubMed:9928952}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:9928952};
CC Multi-pass membrane protein {ECO:0000305}. Host mitochondrion
CC {ECO:0000269|PubMed:16008580}.
CC -!- DOMAIN: The periplasmic domain (residues 221-339) binds peptidoglycan
CC (PGN) and diaminopimelate, one of the components of PGN.
CC {ECO:0000269|PubMed:21965596}.
CC -!- DISRUPTION PHENOTYPE: Significant loss of the bacterial outer membrane,
CC not as able to induce apoptosis as wild-type bacteria in human cell
CC lines. {ECO:0000269|PubMed:16008580}.
CC -!- MISCELLANEOUS: Live A.baumannii and purified Omp38 elicit identical
CC effects with respect to the induction of apoptosis in human cell lines.
CC {ECO:0000269|PubMed:16008580}.
CC -!- SIMILARITY: Belongs to the outer membrane OOP (TC 1.B.6) superfamily.
CC {ECO:0000305}.
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DR EMBL; AY485227; AAR83911.1; -; Genomic_DNA.
DR EMBL; GG704577; EEX02591.1; -; Genomic_DNA.
DR RefSeq; WP_000777878.1; NZ_MJHA01000010.1.
DR PDB; 3TD3; X-ray; 1.59 A; A/B/C/D/E/F/G/H=221-339.
DR PDB; 3TD4; X-ray; 1.79 A; A/B/C/D/E/F/G/H=221-339.
DR PDB; 3TD5; X-ray; 2.00 A; A/B/C/D/E/F/G/H=221-339.
DR PDB; 4G4Y; X-ray; 1.70 A; A/B/C/D/E/F/G/H=221-339.
DR PDB; 4G4Z; X-ray; 1.80 A; A/B/C/D/E/F/G/H=221-339.
DR PDB; 4G88; X-ray; 1.70 A; A/B/C/D/E/F/G/H=221-339.
DR PDBsum; 3TD3; -.
DR PDBsum; 3TD4; -.
DR PDBsum; 3TD5; -.
DR PDBsum; 4G4Y; -.
DR PDBsum; 4G4Z; -.
DR PDBsum; 4G88; -.
DR AlphaFoldDB; Q6RYW5; -.
DR SMR; Q6RYW5; -.
DR TCDB; 1.B.6.1.24; the ompa-ompf porin (oop) family.
DR PRIDE; Q6RYW5; -.
DR EnsemblBacteria; EEX02591; EEX02591; HMPREF0010_02782.
DR GeneID; 66395939; -.
DR PATRIC; fig|575584.18.peg.946; -.
DR eggNOG; COG2885; Bacteria.
DR eggNOG; COG3637; Bacteria.
DR EvolutionaryTrace; Q6RYW5; -.
DR Proteomes; UP000005740; Unassembled WGS sequence.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 3.30.1330.60; -; 1.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR InterPro; IPR027385; OMP_b-brl.
DR InterPro; IPR006664; OMP_bac.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR036737; OmpA-like_sf.
DR Pfam; PF13505; OMP_b-brl; 1.
DR Pfam; PF00691; OmpA; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR SUPFAM; SSF103088; SSF103088; 1.
DR SUPFAM; SSF56925; SSF56925; 1.
DR PROSITE; PS51123; OMPA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Cell outer membrane; Host mitochondrion;
KW Ion transport; Membrane; Porin; Signal; Transmembrane;
KW Transmembrane beta strand; Transport; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..356
FT /note="Outer membrane protein Omp38"
FT /id="PRO_0000290208"
FT DOMAIN 221..339
FT /note="OmpA-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00473"
FT BINDING 237
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000269|PubMed:21965596"
FT BINDING 271
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000269|PubMed:21965596"
FT BINDING 273
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000269|PubMed:21965596"
FT BINDING 279
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000269|PubMed:21965596"
FT BINDING 286
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000269|PubMed:21965596"
FT MUTAGEN 271
FT /note="D->A: Periplasmic domain no longer binds
FT diaminopimelate."
FT /evidence="ECO:0000269|PubMed:21965596"
FT MUTAGEN 286
FT /note="R->A: Periplasmic domain no longer binds
FT diaminopimelate."
FT /evidence="ECO:0000269|PubMed:21965596"
FT STRAND 221..233
FT /evidence="ECO:0007829|PDB:3TD3"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:3TD3"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:3TD3"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:3TD3"
FT HELIX 276..297
FT /evidence="ECO:0007829|PDB:3TD3"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:3TD3"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:3TD3"
FT HELIX 322..328
FT /evidence="ECO:0007829|PDB:3TD3"
FT STRAND 329..339
FT /evidence="ECO:0007829|PDB:3TD3"
SQ SEQUENCE 356 AA; 38420 MW; F6E424870C93C42F CRC64;
MKLSRIALAT MLVAAPLAAA NAGVTVTPLL LGYTFQDSQH NNGGKDGNLT NGPELQDDLF
VGAALGIELT PWLGFEAEYN QVKGDVDGAS AGAEYKQKQI NGNFYVTSDL ITKNYDSKIK
PYVLLGAGHY KYDFDGVNRG TRGTSEEGTL GNAGVGAFWR LNDALSLRTE ARATYNADEE
FWNYTALAGL NVVLGGHLKP AAPVVEVAPV EPTPVAPQPQ ELTEDLNMEL RVFFDTNKSN
IKDQYKPEIA KVAEKLSEYP NATARIEGHT DNTGPRKLNE RLSLARANSV KSALVNEYNV
DASRLSTQGF AWDQPIADNK TKEGRAMNRR VFATITGSRT VVVQPGQEAA APAAAQ
