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OMP52_HAEIF
ID   OMP52_HAEIF             Reviewed;         353 AA.
AC   P38368;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Outer membrane protein P5 {ECO:0000303|PubMed:8359929};
DE            Short=OMP P5;
DE   AltName: Full=Outer membrane porin A {ECO:0000255|HAMAP-Rule:MF_00842};
DE   AltName: Full=Outer membrane protein A;
DE   Flags: Precursor;
GN   Name=ompA {ECO:0000255|HAMAP-Rule:MF_00842};
GN   Synonyms=ompP5 {ECO:0000303|PubMed:8359929};
OS   Haemophilus influenzae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=727;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 22-34.
RC   STRAIN=1613 / Serotype B;
RX   PubMed=8359929; DOI=10.1128/iai.61.9.4017-4020.1993;
RA   Munson R.S. Jr., Grass S., West R.;
RT   "Molecular cloning and sequence of the gene for outer membrane protein P5
RT   of Haemophilus influenzae.";
RL   Infect. Immun. 61:4017-4020(1993).
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   -!- SUBUNIT: Monomer and homodimer. {ECO:0000255|HAMAP-Rule:MF_00842}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00842}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00842}.
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   -!- MISCELLANEOUS: Non-typeable Haemophilus influenzae (NTHi) is a primary
CC       pathogen in otitis media (inflammation of the middle ear).
CC       {ECO:0000305}.
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; L20309; AAA03346.1; -; Unassigned_DNA.
DR   RefSeq; WP_015702094.1; NZ_UEXC01000001.1.
DR   AlphaFoldDB; P38368; -.
DR   SMR; P38368; -.
DR   PRIDE; P38368; -.
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   Cell outer membrane; Direct protein sequencing; Disulfide bond;
KW   Ion transport; Membrane; Porin; Signal; Transmembrane;
KW   Transmembrane beta strand; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842,
FT                   ECO:0000269|PubMed:8359929"
FT   CHAIN           22..353
FT                   /note="Outer membrane protein P5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT                   /id="PRO_0000020108"
FT   TRANSMEM        27..37
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        58..69
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        77..85
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        104..115
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        120..128
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        158..167
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        172..179
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   TRANSMEM        205..213
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   DOMAIN          227..353
FT                   /note="OmpA-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   SITE            80
FT                   /note="Part of salt bridge gating mechanism"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   SITE            175
FT                   /note="Part of salt bridge gating mechanism"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT   DISULFID        326..338
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
SQ   SEQUENCE   353 AA;  37594 MW;  E58A659E7860D0F7 CRC64;
     MKKTAIALVV AGLAAASVAQ AAPQENTFYA GVKAGQASFH DGLRALAREK NVGYHRNSFT
     YGVFGGYQIL NQNNLGLAVE LGYDDFGRAK GREKGKTVAK HTNHGAHLSL KGSYEVLDGL
     DVYGKAGVAL VRSDYKFYED ANGTRDHKKG RHTARASGLF AVGAEYAVLP ELAVRLEYQW
     LTRVGKYRPQ DKPNTAINYN PWIGSINAGI SYRFGQGAAP VVAAPEVVSK TFSLNSDVTF
     AFGKANLKPQ AQATLDSIYG EMSQVKSAKV AVAGYTDRIG SDAFNVKLSQ ERADSVANYF
     VAKGVAADAI SATGYGKANP VTGATCDQVK GRKALIACLA PDRRVEIAVN GTK
 
 
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