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Database: UniProt
Entry: A0A1Z9Z0Z5_9GAMM
LinkDB: A0A1Z9Z0Z5_9GAMM
Original site: A0A1Z9Z0Z5_9GAMM 
ID   A0A1Z9Z0Z5_9GAMM        Unreviewed;       992 AA.
AC   A0A1Z9Z0Z5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Trimeric autotransporter adhesin YadA-like C-terminal membrane anchor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CAP51_00530 {ECO:0000313|EMBL:OUY08143.1};
OS   Acinetobacter populi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1582270 {ECO:0000313|EMBL:OUY08143.1, ECO:0000313|Proteomes:UP000196536};
RN   [1] {ECO:0000313|EMBL:OUY08143.1, ECO:0000313|Proteomes:UP000196536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBJ7 {ECO:0000313|EMBL:OUY08143.1,
RC   ECO:0000313|Proteomes:UP000196536};
RA   Nemec A., Radolfova-Krizova L.;
RT   "Acinetobacter populi ANC 5415 (= PBJ7), whole genome shotgun sequencing
RT   project.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000256|ARBA:ARBA00004241}.
CC   -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC       {ECO:0000256|ARBA:ARBA00005848}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OUY08143.1}.
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DR   EMBL; NEXX01000001; OUY08143.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z9Z0Z5; -.
DR   OrthoDB; 6651929at2; -.
DR   Proteomes; UP000196536; Unassembled WGS sequence.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd12820; LbR_YadA-like; 3.
DR   Gene3D; 6.10.250.2030; -; 1.
DR   Gene3D; 6.10.250.2040; -; 1.
DR   Gene3D; 3.30.1300.30; GSPII I/J protein-like; 1.
DR   Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 5.
DR   InterPro; IPR008640; Adhesin_Head_dom.
DR   InterPro; IPR008635; Coiled_stalk_dom.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR024973; ESPR.
DR   InterPro; IPR045584; Pilin-like.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   InterPro; IPR005594; YadA_C.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1082; COLLAGEN ALPHA-1(X) CHAIN; 1.
DR   Pfam; PF01391; Collagen; 3.
DR   Pfam; PF13018; ESPR; 1.
DR   Pfam; PF03895; YadA_anchor; 1.
DR   Pfam; PF05658; YadA_head; 10.
DR   Pfam; PF05662; YadA_stalk; 2.
DR   SUPFAM; SSF101967; Adhesin YadA, collagen-binding domain; 4.
DR   SUPFAM; SSF54523; Pili subunits; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane {ECO:0000256|ARBA:ARBA00023237};
KW   Membrane {ECO:0000256|ARBA:ARBA00022452};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196536};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane beta strand {ECO:0000256|ARBA:ARBA00022452};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..37
FT                   /note="ESPR"
FT                   /evidence="ECO:0000259|Pfam:PF13018"
FT   DOMAIN          351..371
FT                   /note="Trimeric autotransporter adhesin YadA-like head"
FT                   /evidence="ECO:0000259|Pfam:PF05658"
FT   DOMAIN          374..399
FT                   /note="Trimeric autotransporter adhesin YadA-like head"
FT                   /evidence="ECO:0000259|Pfam:PF05658"
FT   DOMAIN          402..427
FT                   /note="Trimeric autotransporter adhesin YadA-like head"
FT                   /evidence="ECO:0000259|Pfam:PF05658"
FT   DOMAIN          416..442
FT                   /note="Trimeric autotransporter adhesin YadA-like head"
FT                   /evidence="ECO:0000259|Pfam:PF05658"
FT   DOMAIN          432..456
FT                   /note="Trimeric autotransporter adhesin YadA-like head"
FT                   /evidence="ECO:0000259|Pfam:PF05658"
FT   DOMAIN          444..468
FT                   /note="Trimeric autotransporter adhesin YadA-like head"
FT                   /evidence="ECO:0000259|Pfam:PF05658"
FT   DOMAIN          474..511
FT                   /note="Trimeric autotransporter adhesin YadA-like stalk"
FT                   /evidence="ECO:0000259|Pfam:PF05662"
FT   DOMAIN          750..775
FT                   /note="Trimeric autotransporter adhesin YadA-like head"
FT                   /evidence="ECO:0000259|Pfam:PF05658"
FT   DOMAIN          764..787
FT                   /note="Trimeric autotransporter adhesin YadA-like head"
FT                   /evidence="ECO:0000259|Pfam:PF05658"
FT   DOMAIN          793..817
FT                   /note="Trimeric autotransporter adhesin YadA-like head"
FT                   /evidence="ECO:0000259|Pfam:PF05658"
FT   DOMAIN          823..844
FT                   /note="Trimeric autotransporter adhesin YadA-like head"
FT                   /evidence="ECO:0000259|Pfam:PF05658"
FT   DOMAIN          850..890
FT                   /note="Trimeric autotransporter adhesin YadA-like stalk"
FT                   /evidence="ECO:0000259|Pfam:PF05662"
FT   DOMAIN          931..991
FT                   /note="Trimeric autotransporter adhesin YadA-like C-
FT                   terminal membrane anchor"
FT                   /evidence="ECO:0000259|Pfam:PF03895"
FT   REGION          587..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..629
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..686
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   992 AA;  99809 MW;  1FE7C6F4E2C1B929 CRC64;
     MNRIFKTIWN KTLGCMVVAS ELAKSGHATA HSKTTVIPAT SSIAPIFKLS IFVLALSGVI
     ANSVVWASTC TLNGGGNGGS VANTGFSIAC GHSNNISGAF GSAIGVNNNA AGESSNAIGF
     GNKAENKSSN AIGVGNTAES AASNAIGYSN KATGVFSNAI GASNEASGSE SSSIGTNNKA
     SVHLSNAIGS YNKAENEASN AIGYSNEVSG YAGNAVGYAN KALGRDSNAF GSGNTASRDA
     SSALGYSNEA GKNSSAVGFR NKASNEASAV GYVNTASGFQ SSALGNINMA VGVASNAVGS
     FNLASEDYSS ALGYSNKVSE ARSNAVGYMN EALGERNSAV GYNNKTFDEL SSALGANNTA
     ESTNSSAVGY QNTASGSGSN AFGAANQASG DGSSALGSEN TASGIESSAM GFGNIASGGY
     SSAIGYGNTA LADESIAIGY QSEAQAIGST AIGYQAIADR EYTLSVGSVG NERQITHVAA
     GVFDTDAVNL SQIKMLTNGF GGGANFNNGV FTAPTYVIQN NNYQNIGSAF TAVDSKLTSL
     DSRLTTVENN AGGGQGAQGD SAYQVAVNNG FAGTEPEWLT SLKGEQGLQG LKGDQGDKGD
     KGDQGIAGLN GKDGAKGDKG DKGDQGLQGL KGDKGEQGLQ GLQGDQGLKG DQGLQGLNGL
     NGQDGKDGLD GLNGKDGAKG DKGDKGDQGI AGLNGKDGAK GDQGLEGKST FEIAVQNGFQ
     GTEQQWLDSQ TNPYLAIQSN ISKTQSKPQA TGTDAIALGA GAIAQGNQSI SIGVGNKVTG
     HNAGAIGDPN MVSGNDSYAV GNNNSVAGDN TFVLGNNINT QAKNAVVLGN NSTSNRDNTV
     SVGAVDSERQ IIHVAAGTQD TDAVNVKQMK DADTATLKSA QSYADHGNAT TLQSAQRYTD
     SRINHLNQNF KEFKQDTYAA VASSIAIASL PQPSSAGYKM VSIGAGTWKG EQGISIGVSG
     VTENNKFIFK AASTANTQGD FGGGASIGWQ WK
//
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